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273 Cards in this Set
- Front
- Back
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what is the def of physiology?
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how living organisms function
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what is the "dynamic constancy" of conditions found in an organisms internal environment.
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homeostasis
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what happens when things like bp, pH, body temp become too high or too low?
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the body is in anhomeostasis
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why is homeostasis called a dynamic constancy?
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bc it varies over the course of the day
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dose the external environment have an affect on the internal homeostasis of the body?
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yes, but it has to change drastically before having and major homeostasis changes.
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what dose a group of cells make?
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tissue
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t/f: organs help regulate some aspects of homeostasis
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true, usually work with other organs to regulate body
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what are the 1st cells of the body called? what is special about them
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stem cells: they are all the same at first and then differentiate into other cells
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what are the four tissue types?
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epithelial, muscle, nervous, connective
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what is the function of epithelial tissue?
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lines and covers organs and cavities
- secretion, absorption, protection |
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what are examples of epithelial tissues that act in absorption, secretion, and protection?
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absorption: small intestine (food)
-secretion: lining of stomach (mucus, enzymes, acids) -protection: skin (from external environment, sweat glands) |
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why do absorption cells typically have cilia?
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to increase surface area
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what type of cells are cilia and microvilli usually on?
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goblet cells
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what are the functions of muscle tissue?
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specialized to contract, generate mechanical force
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what are the 3 types of muscle tissue and are they voluntary or involuntary?
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skeletal: voluntary
-cardia: involuntary -smooth: involuntary |
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what are the functions of conn tissue?
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connect, anchor, support structures in the body.
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what type of cells are found in the ECM?
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living cells, made of protein fibers (keratin and collagen)
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t/f: all conn tissues have an ECM in btw cells?
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true
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what are the different types of connective tissues?
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loose connective tissue (connects organs to walls),
-dense conn tissue (cartilage) -bone -cartilage -adipose tissue (ECM: fat) -blood (ECM: plasma) |
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is most of the bone cell living or dead?
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dead
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what is most of the fat cell?
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fat, the nucleus and other cells are in the outside of the cell
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what is nervous tissue made of?
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neurons and support cells (glial cells)
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what are the functions of nervous cells?
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generate electrical signals (ap's)
-control activities of other cells |
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what body structures does nervous tissue make up?
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brain, spinal cord, nerves
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what is the function of the kidney?
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filters blood and gets rid excess water and waste
- regulates h2o in the body fluids and other nutrients |
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what types of tissues make up the kidneys?
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many different types!
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what is an organ system?
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groups of organs that work together to perform a particular function
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what is the function of the urinary system?
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regulate amount of water and concentration of other minerals in body organs
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what is the function of teh circulatory system?
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transport: moves food from stomach to other tissues (oxygen from lungs--> cells) (hormones--> body)
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t/f the circulatory does not effect body temp
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false, it DOES have thermal effects
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what structures are involved in the circulatory system?
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blood vessels, heart, blood
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what structures are involved in the urinary system?
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kidney, ureter, bladder, urethra
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what is the function of the nervous system?
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regulate coordination of activities , detect change in a part of the body,
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what does the nervous system consisit of?
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brain, spinal cord, nerves
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what do the brain and spinal cord do in the nervous system?
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act as a integrator and act to clarify information
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t/f: the nervous system helps with memory, organization, and learning?
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true
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what is the function of the endocrine system?
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hormones! and produced by glands and travel through blood until they reach receptor sites
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are the nervous system and endorcine system similar?
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yes, they both react to changes and send out signals (but the nervous system is much faster)
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what consists of the integumentary system?
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skin, hair, nails
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what is the function of teh integumentary system?
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protection and thermal regulation
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what is the function of the respiratory system/
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exchange gasses between body fluids and external environment
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t/f the respiratory system regulates pH?
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true
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what is the lymphatic system?
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system of vessels that carry fluids (lymph) around the body.
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what organs are in the lymphatic system?
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lymph nodes, thymus, WBC
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what are the primary organs of the digestive system? accessory?
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primary: mouth, esophagus, intestines, stomach
accessory; liver, pancreas, gallbladder, spleen |
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what is the function of the digestive system?
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acquire nutrients from food
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musculoskeletal system function?
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more and support the body and thermoregulation
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what does the reproductive system effect?
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growth and development
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what reates the internal environment of the body?
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body fluids, surrounds cells of the body
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what is the intracellular fluid?
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cytoplasm, separates cell membrane and inside of cell (but exchange can occur)
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what are 2 types of extracellular fluids?
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plasma, interstitial fluid (lymph)
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can exchange happen btw plasma and interstitial fluid?
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yes
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what is pathophysiology?
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disease, lack of homeostasis
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which body fluid is the largest in the body?
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intracellular
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between the 2 extracellular fluids, which one is more abundant?
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interstital
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t/f intracellular fluid is only in the body cavities
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false, it is also inside the cell
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all fluids are separated by membranes but can exchange occur?
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yes
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what does intracellular fluid consist of ?
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high concentrations of proteins (enzymes)
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t/f: interstitial fluid and plasma are very different in composition
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false, they are similar, but plasma has more proteins
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what does the body do to reverse pathophysiology?
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has a system of homeostatic controls that balance input/output
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what is the primary form of homeostasis
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negative feedback
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what is negative feedback?
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a change in a variable that causes a response in teh body that causes the variable to change in the opposite direction
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what is the biochemical pathway?
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how most things in the body get developed
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what is positive feedback?
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change in variable causes the variable to change even more in the same direction (breast feeding)
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what is feedforward?
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a compensatory responses are activated before a change in a variable occurs
-occurs when your body is anticipating a change |
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what is an example of feed forward?
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skin feels old and causes shivering before body temp drops
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what is a reflex? and how do they occur?
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an involuntary, unpremeditated, unlearned "built in" response to a particular stimulus. they occur through a reflex arc
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in a reflex does the stimulus reach the brain?
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no
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are reflexes learned or acquired?
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they can be both
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what does the integrating center in the reflex arc do?
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receives data and figures out what to do
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in the efferent pathway what does the effector do?
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changes the variable back to normal (produces a response)
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what is the role of the afferent pathway?
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1st step: goes from the stimulus to the integrating center
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what are the local responses?
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1 cell or tissue that releases chem messengers to nearby cells (paracrine)
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are paracrine and autocrine substances often the same?
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yes because it also effects itself.
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what does the autocrine substance do
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releases chem messenger and effects itself
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can a cell be effected by the hormone if it doesnt have the receptor sites?
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no, the cell must have receptor sites
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what does adaptation mean:
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denotes a characteristic that favors survival in specific environments
(an evolutionary change to a change in response to ones environments) |
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is adaptation or acclimatization more permanent?
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adaptation
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what is acclimatization?
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the improved functioning of an already existing homeostatic system baed on an environmental stress
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can variables change throughout the day?
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yes
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if ouput is more that input what happens to the total amount of substance in the body? if input is greater than output?
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output>input: amount dec in total pool
input> output; amount increase in total pool |
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what are molecules?
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a group of atoms held together by energy
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what is the energy holding two atoms together called?
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chemical bond
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what are the 3 main types of chem bonds?
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ionic, covalent, hydrogen
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what is an atom called that loses or gains electrons?
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and ion
(if lost electrons= pos ion, if gained electrons= neg ion) |
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what does and ionic bond involve?
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attraction of opposite electrical charges
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what is the structure that molecules combine to make and are most stable in this state?
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crystals
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what type of bond is formed between two atoms when they share electrons?
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covalent bonds
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t/f the number of electron shared is always the same amount
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false, it varies depending on how many the atom needs to fill its outermost shell
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are covalent or ionic bonds stronger?
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covalent
(ionic bonds will break in h2o but covalent wont) |
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what is it called when one nucleus attracts the shared electrons more than another nucleus?
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a polar covalent bond
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what is the affinity for electrons by a nucleus called?
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electronegativity
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polar molecules?
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are molecules with partial charges in the atoms that are unequally sharing electrons
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which type polar/nonpolar dissolves in water?
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polar is soluble in water
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in non polar bonds do either of the atoms have a greater affinity towards the electrons?
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no
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t/f water is polar
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true
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what are hydrogen bonds?
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they form between the positive end of one polar molecule and the negative end of another
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what happens when there are multiple hydrogen bonds in one place?
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will make them all collectively stronger
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what is an ex of a hydrogen bond?
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water
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what does hydrophilic/ hydrophobic mean?
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hydrophilic: love water (can dissolve in h2o)- polar
hydrophobic: repelled by water (cannont dissolve in h20)- non polar |
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what are amphipathic molecule?
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have a polar and non polar end
(forms the basic idea for cell membranes |
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substances dissolved in a liquid are known as
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solutes
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what is a solvent
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the liquid in which solutes are dissolved
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what is a solution
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what is formed when solutes dissolve to form a solution
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what is ionization?
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when a H+ ion breaks off forming a OH- and H+ ion
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ionization spontaneously happens to a number of water molecules which causes what?
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causes water to have a neutral pH (pH 7)
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if you have an excess of free H+ ions what type of solution is formed? and excess of free OH-?
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H+: acidic,
OH- : basic |
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what is the pH scale measure
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hydrogen ion concentration
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10^-8??
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pH 8
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an acidic solution is capable of donating or taking up H+ ions?
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donating
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what is a buffer?
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a chemical substance that takes up or releases hydrogen ions
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do buffers remove the acid/base from the solution/
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no they minimize their effect on pH
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what is the most common buffer in the body?
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bicarbonate H2CO3
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what are organic molecules?
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formed by living organisms. they are made of carbon chains (backbones)
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what differs the organic molecules?
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the functional groups attached to the carbon backbones (fgroups= confer specific chemical properties on the organic molecules)
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what are the building materials of the body? they are very large
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macromolecules
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what are the 4 main types of macromoleucles?
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proteins, nucleic acids, carbohydrates, lipids
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t/f macromolecules are not polymers?
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false: they are considered polymers bc they are made up of smaller subunits (monomers)
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what are the monomers of proteins?
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amino acids
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nucleotides are the monomers for what polymer?
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nucleic acids
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what are the monomers for carbohydrates?
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simple sugars... BUT carbohydrates themselves are monomers for simple/ complex carbohydrates
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fatty acids are monomers for what macromolecule?
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Lipids
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how are all polymers assembled?
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by dehydration synthesis
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what is dehydration synthesis?
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when two subunits are combined by removing a hydroxyl (OH-) group from one and a hydrogen (H+) group from the other (ends in a removal of a water (h2o) molecule)
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how are polymers disassembled into monomers?
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by hydrolysis (adding h2o to a polymer will break it up into monomers)
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what links two amnio acids together? and what is this bond called?
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covalent bonds link them together, they're called a peptide bond
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what is the assembled protein polymer called?
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polypeptide
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what is an amino acid made of?
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an amine group (H-N-H), a hydrogen, and carbocylic acid (O=C- OH-)
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what is the only difference btw all amino acids? and what does it do for the amino acid?
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the R groups
(functional groups)- it gives the amino acids their chemical identity |
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what does an amine group look like?
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H-N-H (NH2)
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what does a carboxyl group look like
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O=C-OH-
(-COOH) |
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what are the functions of proteins?
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-makes enzymes
- forms structure (building blocks of nails, hair) - forms cartilage (ears, nose) - helps provide energy - acts as a carrier molecule (hemoglobin- O2) - is in a # of hormones and chem messengers (insulin) - in all cell membranes (membrane proteins) |
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why can proteins bind to chemicals? and what does it allow them to do?
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their shape allows them to bind to certain chem, this allows them to complete all of their functions
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what is a proteins primary structure?
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the sequence of amino acids in the polypeptide chain (determines all other levels)
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why does a secondary structure of a protein form?
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bc regions of the polypeptide that are non-polar are forced togehter; hydrogen bonds form btw diff parts of the chain
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what are the different forms that secondary structure of proteins can be?
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coils, helices, or sheets
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what is tertiary structure of proteins?
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the final 3-D shape of proteins
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what causes the final twists and folds that lead to the tertiary structure of a protein?
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the polarity differences in regions of the polypeptide
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does the same protein always fold in the same ways or can it be different each time/
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a protein always folds in the same way
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what is the quaternary structure of proteins?
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the spatial arrangement of portiens comprised of more than one polypeptide chain
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what is an example of a quaternary structure protein?
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hemoglobin
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what happens when a protein loses its shape
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it is denatured
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t/f temp and pH change can lead to denaturation of a protein
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true- they affect hydrogen bonding- which is involved in the folding process
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what type of proteins are enzymes
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globular proteins that have a special 3-d shape that specifically with a chem reactant
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what are reactants?
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substrates in chem reactions
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what do nucleic acids do?
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they are long polymers hat store information
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what are all nucleotides comprised of?
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5-carbon sugar, phosphate group, organic nitrogen-containing base
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how many diff types of nucleotides are there?
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5: adenine, guanine, cytosine, thymine, uracil
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what are the purine bases?
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A and G (adenine and guanine)
they all end in -ine (and have double rings of nitrogen and carbon atoms |
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what are the pyrimidine bases?
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cytosine and thymine only have a single ring
(all have "y's" |
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what are the 2 types of nucleic acids?
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DNA and RNA
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which part of the nucleotide contains the information to code info
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the bases: ATCG
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which part of the nucleotide makes up the backbone of the double helix
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the phosphate group and 5-carbon sugar
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what is another type of purine base? and what is its importnat function?
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ATP- stores energy
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what is a carbohydrate?
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a monomer that makes up the structural framework of cells and plays a critical role in energy storage
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what are simple carbs? complex?
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simple: consists of one or 2 monomers (monosaccharides/ disaccharides)
complex : long polymers (glycogen) (polysaccharides) |
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what is special about complex carbohydrates?
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only plants can make them
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what is an example of a monosaccharide? disaccharide?
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monosaccharide: glucose
disaccharide: glucose+fructose= sucrose (table sugar) |
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how are di/ polysaccharides formed/
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through dehydration process
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what are complex carbohydrates good for doing?
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storing energy, in their C-H bonds (long term energy storage)
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what are lipids?
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fats and other molecules that are not soluble in waters
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what are the 3 main types of lipids were focusing on?
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fats, oils, steroidss
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what are the 2 subunits of lipids?
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fatty acids (3) and glycerol
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what are fatty acids composed of?
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C-H atoms known as hydrocarbons (the chain always ends in a carboxyl (-COOH) group
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what is the other name for fat?
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triglyceride bc there are 3 fatty acid cains
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what types of lipids are saturated/ unsaturated? and what does that mean?
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saturated: FAT: all single bonds
- unsaturated: OIL: kinky, double bonds |
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t/f fats are liquid at room temp and oils are solid?
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false; fats: solid, oils: liquid
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why are unsaturated lipids oils?
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bc the double bonds make it kinky and dont allow the molecules to come togehter to make a solid
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what type of lipid is best for a diet?
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polyunsaturated
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what are the 3 needs/ uses of cholesterol?
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1. every cell needs cholesterol (cell membrane structure)
2. all steroid hormones are derivatives of cholesterol (estrogen, testosterone) 3. liver produces bile to diges fats (cholesterol makes bile) |
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what are the functions of lipids/
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store long term energy, make up phospholipids in membrane
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what is in the endomembrane system?
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rough, smooth er, golgi and nuclues
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t/f all membranes in the cell are phospholipid bilayers
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true
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what is the function of teh cell membrane?
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regulates moving substances in/out of cell to help maintain homeostasis.
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what are glycoproteins function?
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cell-cell recognition (immune system)
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what are membranes composed of?
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phospholipids (amphipatic molecules)
- cholesterol, -membrane proteins |
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what part of a phospholipid is hydrophilic?
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the phosphate makes the polar head
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what part of the phospholipids are hydrophobic?
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the fatty acid chains (2)
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what are integral membrane proteins?
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they are amphipathic molecules that help transfer molecules in/out of cell (the amphipathic part helps hold protein in place)
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what are integrins?
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peripheral membrane proteins (not amphipathic).
can be on the inside or outer surface. - they help bind extracellular matrix o intracellular matrix |
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what are the 3 types of membrane junctions?
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-desomsomes
- tight junctions -gap junctions |
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what are the functions of the desmosome?
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really strong!
- usually with skin cells bc it allows them to stretch and withstand pressure |
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what are the characteristics of tight junctions?
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quilted, look stitched,
- little/ no space btw cells (epithelial tissues, so most substances cannot get through) |
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what are the characteristics of gap junctions/
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proteins lik the cytosols of adjacent cells.
- important in cardiac muscle |
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what organelle of the cell contains DNA which has the genes to code for proteins (cell functions)
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Nucleus
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what is the nucleus surrounded by?
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nuclear envelope with pores to let MRNA and other things in/out
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what are some functions of teh smooth ER
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contains enzymes for fatty acid and steroid synthesis; stores and releases Ca+
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what does the golgi apparatus do
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concentrates, modifies and sorts proteins and then ships them off in vesicles
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what is the diff btw exocytosis and endocytosis?
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exo- leaves cells,
endo- enters cels. |
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what is the function of mitochondria?
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cellular respiration, makes ATP, has its own DNA, double membrane (inner has enzymes on it- helps with ETC)
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wha tis the function of the cytoskeleton?
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anchors organelles in place/ helps them move.
- gives cell structure - |
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what are the 3 main components of the cytoskeleton
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microfilaments, intermediate filaments, microtubules
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what are some characterisitics of microfilaments?
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muscle fibers,
- help determine shape, -cell division - move cell in amoeba function -contract muscles |
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what are cilia
|
hair like extensions
- are in the trachea to help move mucous out. |
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what causes cilia and flagella to move
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interactions btw microtubules
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what is the only cell in the body with flagella?
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sperm
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when MRNA leaves the nuclues where does it go?
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to the Rough ER
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are lock and key bonding like covalent bonds
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no, they are loose bonds
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t/f a protein only has 1 binding site
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false, it can have multiple
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substrate vs ligand?
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substrate is a ligand!
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how do enzymes bind?
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bc shapes fit together and charge differences and polarity diff
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can any ligand bind to any protein?
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no, they are specific. but some can be more/ less specific
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does affinity affect the strength of a protein bond ?
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yes, if there is a low affinity bonding site it wont be a strong bond.
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if a binding site is full it is 100% saturated. is there anyway to inc saturation?
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no, you could only inc the number of proteins available
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t/f if the protein and ligand have a high affinity the saturation will occur at alot lower concentration of protein
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true
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what characteristic does an allosteric protein have special?
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at least 2 binding sites
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what is the diff btw allosteric and active binding sites?
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active: where the substrate binds,
allosteric: regulates binding of protein and substrate |
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does a phosphate bidning to protein through covalent bonds effect the enzyme
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yes!
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what is the term for the breakdown of organic molecules
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catabolism
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what is teh synthesis of organic molecules?
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anabolism
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t/f heat is only generated during catabolic reactions?
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false, it is created in both
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what 4 things determine the rate of chemical reactions?
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1. reactant concentrations
2. activation energy 3. temperature 4. catalyst |
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if there is higher concentrations of reactant/ product what does it do to the reaction rate?
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increases reaction rate
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what does higher activation energy do to the reaction rate?
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slows down the reaction rate
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does a higher or lower temp increase the reaction rate?
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higher temp
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t/f chemical reactions can only occur in one direction
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false, they can be reversible sometimes.
in reversible reactions- at equilibrium, product conc are slightly higher than reactant |
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what is the direction of a chemical reaction is determined in part by the concentrations of reactant and product?
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law of mass action
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in a reversible reaction, according to the law of mass action, if you increase the concentration of the reactants then what will happen to the equation?
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it will go from left to right, and you will get more of the products
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can an enzyme get used up in a chemical reaction
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no, it stays the same, but substrate changes
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what is the job of an enzyme in a chemical reaction
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to lower the activation energy needed to start a chem reaction
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what are the 2 main things that affect a chemical reaction
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1. enzyme and substrate concentration
2. enzyme activity |
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what are the characteristics of an enzyme
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1. undergoes no net chemical change
2. enzyme and substrate= protein and ligand 3. enzyme inc the rate of reaction but doesnt cause it to occur 4. some enzymes inc both the forward and reverse rates of a chem reaction, they dont change the equilibrium reached only make it reached faster 5. lowers the activation energy of a reaction but doesnt change the net energy |
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what are cofactors? coenzymes?
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cofactors; metal ions
- coenzymes: organic molecules (usually vitamins) they both bind to enzyme and help turn it on/off |
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how are multienzyme reactions regulated/
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by negative feedback loop- it inhibits enzymes by allosteric sites when enough product is made
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what are the reactants, prodcuts and pay offs of glycolysis?
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reactant: glucose (6 carbons)
product: 2 pyruvates (3 carbons) payoff: ATP and some coenzymes |
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when you add O2 to pyruvate what happens?
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acetly CoA is made --> krebs cycle
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what are the reactants, products and pay offs of the krebs cycle?
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reactants: Acetyl CoA
products: CO2 pay off: the energy form the Acetyl CoA being oxidized and binding to NADH and FADH2 |
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if no O2 is added to the pyruvate, what happens
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it undergoes fermentation to make lactate
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what are the reactant, product and pay off of pyruvate oxidation
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reactant: pyruvate
product; acetyl CoA pay off: NADH |
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what do you start off with, end with in ETC
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start with NADH and FADH2, and end with H+ gradient and H2O as a net result. (the H+ gradient leads to lots of ATP generation)
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what does the ATP synthase enzyme allow?
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allows the high concentration of H+ to enter into the other side of the ETC- creating ATP
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what is the end products of carbohydrate catabolism (cellular respiration)?
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6CO2 + 6 H2O + 34-38 ATP
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what does glucose turn into to keep long term storage in the body?
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glucogen- which can be activated to relensih low glucose levels
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what is gluconeogenesis?
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how the body makes glucose from things that are not subar
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t/f you can make glucose from pyruvate?
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true and from oxalcetate ?
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what can Acetly CoA make?
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fatty acids vie versa
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what happens to the NH3 from the amino acids pools?
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it is sent to the liver to make urea and is exported out through urine
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what is deamination? and what does it do?
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taking off an amino group, it is a way to metabolize an amino acid
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what is formed when you deaminate an amino acid?
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you get a keto acid
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What happens to the ammonia that is made form the deamination process?
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it is sent to the liver and turned into urea
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t/f in transamination you don not lose any amino acid?
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true, instead of popping off an amino group, it is transferred o a keto acid to make the needed aa.
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what are two examples of keto acids?
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pyruvate and alpha ketoglutaric acid (both from glucose breakdown- glycolysis)
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t/f pyruvate can only be used to start the krebs cycle?
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false, it can also be used to form an amino acid.
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t/f: pyruvate is formed when you catabolize an aa?
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true it is then used in the krebs cycle
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what is the most efficient way to store long term sugars/carbs? why?
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fat- it has more calories so it stores more
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are all essential amino acids produced inthe body?
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no, only 11- the other 9 we need to get from our diet.
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what is the term for the movement of molecules from high concentration to low concentration?
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diffusion equilibrium
(there is a net mvmt- meaning the molecules move all directions but more towards the side with less) |
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what are the 3 limitations to getting through a membrane?
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1. how big the molecule is (only small can sneak through)
2. only hydrophobic (nonpolar) molecules cant get through 3. the charge or not (ions cannot fit) |
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the membrane proteins for charge particles are called ion channels, what do they do?
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help move ions through the membrane with out going directly through the lipid bilayer.
- they can be very specific (size and charge) |
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how does a membrane potential happen?
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by having an imbalance of pos/neg charge across the cell
- generally: inside is slightly neg and outside is positive |
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what are the 2 forces that effect mvmt through the membrane
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1. chemical gradient (ions go from high conc--> low)
2. electrical factors (like factors repel, different attract) |
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what happens when you have a large number of ions on one side of the membrane and none on the other?
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potential energy develops
- it is used to do work and represents a flow of charge (electrical current) |
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what are teh most common cations and which one is found in/out of the cell?
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intracellular: Potassium (K+)
extracellular: Sodium (Na+) |
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what are the most common anions and which one is found in/out of the cell?
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intracellular: neg proteins (dont move out of the cell)
extracellular: Chlorine ions (Cl-) |
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what are the 3 types of gated channels?
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1. ligand gated
2. electrically gated/ 3. mechanically gated |
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how does a ligand gated channel open?
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when a ligand attaches the the channel it causes it to open (or close depending on stimulus) allowing the molecules to rush in (or out) of the cell
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what happens in an electronically (voltage) gated channel?
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the cell membrane's potential energy changes causing the channel to open/close.
- the membrane potential changes bc of a ligand attached to a ligand channel earlier in the membrane |
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what allows mechanically gated channels to open/close?
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some type of physical stimulus, which allows the ions to rush in
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what happens in mediated transport? (facilitated transport)
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the transporter protein has a binding site that allows the ions to attach to it and is then brought through a channel into the cell. (still diffusion- can only go 1 way).
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with mediated transport can a maximum flux into the cell be reached?
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yes bc the carrier proteins can become saturated and plateau
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what is active transport?
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allows molecules to travel against their concentration gradient
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does active transport require energy?
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yes ATP (usually the carrier protein has multiple sites for ATP, molecule, and a coenzyme)
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what is an ex of a primary active transport?
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sodium potassium pump
- has 3 binding sites for Na+, 2 binding sites for K+, 1 binding site for ATP |
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what is the role of the sodium potassium pump?
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to pump 3 sodiums out, 2 potassiums in at the expense of 1 ATP
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what is secondary active transport?
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when there are 2 substances, and 1 moves against the concentration gradient- and the other moves with the concentration gradient.
(the energy from the Na+ moving with the concentration gradient produces the energy required to move glucose against concen gradient_ |
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what is cotransport? countertransport?
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cotransport: material move in the same direction
countertransport: material moves in opposite directions |
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what is osmolarity?
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the total solute concentration of the solution
1 osmole= 1 mol of particle |
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t/f as the osmolarity inc the concentration of H2O dec?
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true
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what is osmosis?
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diffusion of water across a semipermeable membrane
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what are the 2 functions of exocytosis?
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1. transport molecules out of cell
2. inc size of cell membrane |
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what are the 3 types of endocytosis?
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1. pinocytosis (liquid)
2. phagocytosis (solids) 3. receptor mediated: membrane proteins with attached substance is brought into cell |
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what are the 2 ways to fit through epithelial cells?
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1. paracellular (in between cells)- have to be really small
2. transcellular (through cells)- most common! |
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t/f: when transporting substances out of the gut they have to pass through 2 mebranes (of the epithelial cell) and can use 2 diff types of mvmt methods
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TRUe
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