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104 Cards in this Set

  • Front
  • Back
4 Biomolecules
1. Protein
2. Carbohydrates
3. Lipids
4. Nucleic Acids
Common medium for Rxns
Water
Products of Metabolism
CO2 and H2O vapor
Respiration in relation to chemistry
Controlled Combustion Rxn
Def. of Protein
A large biological molecule of multiple amino acids linked via AMIDE (peptide) bonds
Def. of Amino Acids
Protein building block.
A molecule that contains both an AMINE group & CARBOXYLIC ACID functional group
Fxn of Protein Enzyme and ex
Catalyze reaction
ex: Urease
Fxn of Protein Hormones and ex
Maintain homeostasis
ex: insulin
Fxn of Protein Storage and ex
Store O2 in muscle
ex. Myoglobin
Example of a Protein used in Transportation
Hemoglobin
Fxn of Protein used for Structure and ex
Shape and support
ex. collagen
Ex of Protein used for Protection
Immunoglobulins
Protein used for Motion
Contractile proteins
Actin & Myosin
Def of Amino Acid
the group bonded to the carbon atom next to the carboxyl group (alpha carbon)
- vary in size and shape
- Determines the acid/base nature of the 20 amino acids
All Amino Acids is Proteins are?
in L-configuration b/c the enzyme that make protein will only insert L-amino acids
Primary Structure of Protein
- Sequence of amino acids
- amino acid residue = single amino acid on peptide chain
- remove H2O causes AMIDE bond
- repeating back bone of carbon and nitrogen
- sequence of amino acid is genetically pre-determined
Secondary Structure of Protein
- regular & repeating patterns
- created by hydrogen bonds
- Hydrogen bond connects CARBONYL Oxygen of 1 peptide bond with AMIDE Hydrogen of another nearby bond
- this bonding causes Helix shape
- Amino Acids are closer together than in Primary Protein structure
Tertiary Structure of Protein
R group bond or interactions among R groups that are further apart on the chain
Quaternary Structure of Protein
2 or more Peptide chains aggregate to form a complex structure
Protein Hydrolysis
* Loss of Primary Structure
- the reverse of protein formation
- Peptide bonds break with the addition of H2O
- Results in individual Amino Acids
- Digestion of protein occurs in this way
Protein Denaturation
* Loss of Secondary, Tertiary, and Quaternary structure
* Primary Structure remains
- Properties of the protein changes
- usually irreversible
- causes include heat, mechanical agitation
ex: cooking an egg
Hemoglobin
- Quaternary Structure essential to fxn
- 4 polypeptide chains (2 alpha & 2 beta)
- Heme (4 units)
- Amino acid substitution
- Electrophoresis determines the type of Hgb
Heme
Organic component with Iron (Fe) atom
Sickle Cell Anemia
- Hereditary dx, genetic defect
- Replaces 1 amino acid (Glutamine) in each of 2 beta polypeptide chains of HgbA with another amino acid (Valine)
- HgbS replaces HgBA
- RBC sickle and are fragile and block capillaries
Sickle Cell Trait
- HgbA inherited from 1 parent and HgBS from other parent
- Patients are usually healthy
Phenylkentonuria
- Absence or deficiency of phenylalanine hydroxlylase
- Phenylalanine accumulated (75% is usually convereted to tyrosine)
- Autosomal recessive transmission
Tyrosine is precursor to what 2 Neurotransmitters
Epi and Norepi
Albinism
- Lack of enzyme tryosinase
- Lack of melanin in melanocytes
- Autosomal recessive transmission
Prion Disease
- Brain protein converts to altered form
- Alteration occurs in secondary protein structure
- Creutzfeldt-Jacob disease
- Mad Cow dx
Prion
Proteinaceous infectious particle affecting Prion
Histamine is amino acid for what?
Histidine
Porphyria
- Porphyrin synthesis ultimately results in heme for Hgb
- Series of enzymatic rxns & deficiency of enzyme causes porphyria
- Any increase in heme requirements causes accumulation of intermediated in this pathway
- Affect CNS and PNS
- Porphyria causes triggering of acute result in weakness autonomic nerve sys. dysfxn, Result in: Labile hypotention, death from resp. muscle paralysis, severe emotional disterbences, and psychosis
- R/T Cytochrome P450
* Avoid: Thiopental, Barbs, Ethyl Alcohol, Ketamine, Etomidate
Enzymes
- Catalyze chem rxn
- water soluble globular protein
- larger and more complex than inorganic catalyst
- decreases energy of activation and speeds up rxn
- most biologic rxn doen't take place at perceptible rates w/o enzyme
- Often highly specific for rxn or grp rxn
Carbonic Anhdrase
* Enzyme Catalyst
- catalyzes the hydration of CO2 & H2O to H2CO3 (carbonic acid)
- can hydrate 1 million molec. of CO2 per second
- Enzyme speeds rxn 10 million times
Cholinesterases
* Enzyme Catalyst
- Ex: Acetylcholinesterase = True cholinesterase
- Ex: Plasma Cholinesterase = Pseudocholinesterase
Acetylcholineserase
- break down Ach and splits it into Acytate ion & Choline
- present in nerve ending & on surface of receptor organs (end organs) to break down Ach
Plasma Cholinesterase
- responsible for hydrolysis of Succinylcholine
- made in liver and found in plasma
- most Succinylcholine is metabolized before getting to nerve endings b/c of plasma cholinesterase
Atypical Plasma Cholinesterase
Causes prolonged effect of Succinylcholine
Mech of Action of Enzymes
- lock and key mech
- active site on enzyme attracts and holds substrate
active site
pocket on enzyme
substrate
reactant in rxn that is catalyzed by enzyme
Effect of Concentration of Rxn Rate
- increases the concentration of enzyme or the substrate increases the rxn rate up to the point where the enzyme is saturated
- ex: direct relationship btwn rate of rxn & substrate concentration
- pH btwn 5-9 is where max enzyme activity happens
2 Enzyme Regulations
1. Competitive Inhibition
2. Noncompetitive Inhibition
Chemical Messengers
1. Hormones
2. Neurotransmitters & Receptors
Hormones
- chemical messengers of the endocrine system
- transported via blood target organ
2 Classifications of Hormones
1. protein derivatives
2. Lipid derivatives
2 Protein derivative hormones
1. Amino acid derivatives
2. Polypeptides
1 Lipid derivative hormone
Steroids
ex: cortisol and aldosterone
Autonomic Nervous System
- activated by the Hypothalamus, brain stem, and spinal cord
- Presynaptic (pregangiolonic) neuron & postsynaptic (postganglionic) neurons
Neuromuscular Junction work on:
- work on neuron end @ end organ
Sympathetic N.S.: PREsynaptic (preganglionic) neurotransmitters
- Acetylcholine
- Cholinergic
Sympathetic N.S.: POSTsynaptic (postganglionic) neurotransmitters
- Norepi
- Adrenergic
Parasympathetic N.S.: PREsynaptic neurotransmitters
- Acetylcholine
- Cholinergic
Parasympathetic N.S.: POSTsynaptic neurotransmitters
- Acetylcholine
- Cholinergic
2 Cholinergic Receptors
1. Muscarinic
2. Nicotinic
Muscarinic Receptor:
location
agonist
antagonist
-Location: END ORGANS, including glands, smooth muscle, and nodes in heart
- Agonist: Acetylcholine
- Antagonist: Antimuscarinics = Atropine, Scopolamine, Glycopyrolate
Nicotinic Receptor:
location
agonist
antagonist
- Location: Autonomic glanglia, skeletal muscle
- Agonist: Acetylcholine
- Antagonist: Nondepolarizing muscle relaxants, Ganglionic blockers
The only depolarizing muscle relaxant
Succinylcholine
Adrenergic Receptors
- Neurotransmitter is Norepi (mostly)
- Norepi is synthesized in the cytoplasm then packed into vesicles in postganglionic fibers
- released by exocytosis
Adrenergic Receptor Action Terminated by:
1. Reuptake into the postglanglionic nerve endings
2. Diffusion away from the receptor
3. Metabolism by MAO and COMT
Alpha-1 Adrenergic Receptors
- Postsynaptic
- locate in smooth muscle throughout the body, in the eye, lung, blood vessels, uterus, gut, & GU system
Alpha-2 Adrenergic Receptors
- Presynaptic nerve terminals
Beta-1 Adrenergic Receptors
- Postsynaptic membranes in the heart
Beta-2 Adrenergic Receptors
- Postsynaptic in smooth muscle and glands
2 Sympathomimetics
1. Ephedrine
2. Phenylephrine
Ephedrine
- Mixed acting sympathomimetic
- react with Alpha and Beta
- Indirect and Direct action
Phenylephrine
- Direct acting
- Alpha agonist
Neuromuscular Blocking Drugs
1. Depolarizers (agonists)
2. Nondepolarizers (antagonist for Ach & neuromusclular jxn)
Pseudocholinesterase deficiency
- Inherited disorder
- Prolonged blockade following suxxinylcholine
- Homozygose: block lasts 3hrs or longer
- Heterozygose: block lasts little longer than normal
Histamine
- Neurotransmitter
- Naturally occurring AMINE
- H1 receptor
- H2 receptor
- H3 receptor
H1 Receptor
- smooth muscle contraction in respiratory & GI tracts
H2 Receptor
- Stimulation of gastric hydrogen ion secretion
H3 Receptor
- Stimulation causes inhibition of synthesis & release of histamine
- action may be impaired by H2-receptor blockers increasing histamine release with certain meds ex: atracurium
Carbohydrates
- Aldehydes or Ketones with multiple OH groups
- Most of organic matter on earth
- Extensive roles in all forms of life
- Monomer unit is a monosaccharide
- General formula for a monosaccharide is: C-H2O or literally a "carbon hydrate"
- 3-9 carbons
- Polysaccharid = monosaccharides linked
- Exist as Enantiomers ex: dextrose = change in glucose
Role of Carbohydrate
- Energy store
- Fuels
- Metabolic intermediates
- Structural framework of DNA/RNA
- Structural elements of cell walls
- Mediators of cellular interactions
Metabolism
- series of linked rxns
1. take digested Carbohydrates & convert to simple surgars by amylase in mouth
2. Pancrease secretes amylase too
3. Sugars move to liver & other tissue and convert to fatty acid, amino acid, and glycogin
*Food (fuel) + Inspired air (O2) = Energy
Catabolism
- brk down of fuel sources by:
1. oxidation of food molecules to produce fuel
2. Convert fuel into cellular energy
Anabolism
- Build up of body tissue from dietary sources
Energy Production
- Produced by the oxidation of biomolecules consisting mainly of carbon, hydrogen, and oxygen
- End products are CO2, H2O, and energy (ATP)
- CHO, proteins, & lipids differ in structure & broken down in different initial pathways but all end up in the citric acid cycle & oxidative phosphorylation
Building Block of Lipids
fatty acids
Building Block of Carbohydrates
Gycolosis
Building Block of Protein
Amino Acids
Mitochondrion
- cell power house
- 90% ATP produced
- have own DNA
- reproduce to aid in energy production
Glycolysis
- occur in cytoplasm
- series of rxns that convert 1 molecule of glucose into 2 molecules of pyruvic acid + energy (ATP)
Acetyl Co-A
- intermediate in the breakdown of all classes of food molec
- carries the Acetyl groups into the common pathways of catabolism - citric acid cycle & electron transport, ATP production
- also used in the synthesis of Ach
Citric Acid Cycle
- Tricarboxyl acid cycle (TCA)
- Kreb's Cycle
- common pathway for oxidation of fuel molec which enter the TCA as acetyl CoA
- Breakdown of acetyl group (from acetyl CoA) into 2 moelc of CO2 + energy carried by reduced coenzymes
- Primary fxn is the harvesting of high energy electrons to enter oxidative phosphorylation and ATP generation
Fat, Sugar, and Protein all breakdown to make?
Acetyl CoA that moves into the Kreb's Cycle
Oxidative Phosphorylation
- occurs in mitochondrion
- high energy electrons from the citric acid cycle
- Occurs in a number of electron-transfer rxns which take place in a set of membrane proteins known as the electron transport chain (respiratory chain)
- ATP is formed
ATP
- Energy transporting molec
ATP production from ADP (phosphorylation) requires an input of energy which is then released whenever the reverse rxn occurs
- ATP hydrolysis releases energy
Complete metabolism of 1 mole of glucose through glycolysis & the citric acid cycle yields how many ATP
36-38 ATP
the from Anaerobic glycolysis in which glucose is converted to lactate in a net of how many ATP
2 ATP with anaerobic glycolysis
How much ATP can be produced with 1 glucose molecule
30-32 ATP/glucose molec
Gluconeogenesis
making of glucose from amino acid and fatty acid
Metabolic Effects of Trauma and Surgery
1. Glycemic response = Hepatic glycogenolysis & gluconeogenesis

2. Protein catabolism = Amino acid released & weight loss up to 0.5kg of lean body mass per day
Lipids
- Naturally occurring molecule from a plant or animal that is soluble in nonpolar organic solvents but not in water
Structure of Lipids
- ESTERS and AMIDES of Carboxylic acids
- Long, straight chain hydrocarbons (fatty acids)
- ex: Steroids = basic structure
Roles of Lipids
- Energy storage
- Cell membrane (lipid bilayer)
- Chemical messangers
Membrane Lipids
1. Phospholipids = basic structure of cell membrane
2. Glycolipids
3. Cholesterol = form membrane
Composition of Cell Membrane
- Phospholipid bilayer
- includes cholesterol, proteins (including glycoproteins), & glycolipids
Permeability & Transportation across the Cell Membrane
- Simple vs. facilitated diffusion
- Active transport
Components of Body Fluid
1. Intracellular fluid = 64%
2. Extracellular fluid = plasma & interstitial fluid = 33%
3. Interstitial fluid = 25%
4. plasma = 8%
Regulation of fluid Balance
1. I & O
2. Kidneys
3. Hormone secretion (ADH)
Role of Kidneys in Fluid Balance
Maintain H2O & electrolyte balance by increasing or decreasing amounts eliminated mediated by Hormones such as ADH
2 Types of Hormones that affect Fluid Balance
1. Osmoreceptors = in hypothalmus
2. Aquaporins