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47 Cards in this Set

  • Front
  • Back
regulation of your internal environment to face the changing external environment
Opposite of homeostasis. Allows parameter to change with external environment
Membrane function
1. separate intracellular and extracellular spaces
2. Separates organelles from cytoplasm
3. Epithelium separates from environment
4. Regulates exchange with environment
5. Communicates with environment
6. Structural Support
Two types of membrane proteins
peripheral and integral
What is a CHO group used for within the membrane?
signaling and immune signals
Aids in the fluidity of the membrane during times of colder temperature by unsaturation of the lipid molecules
Four types of tissue
Connective, Muscle, Nervous, Epithelial
Two types of extracellular fluid
Plasma, interstitial fluid
Three types of Junctions
Gap Junction, Tight junction, Anchoring junction
Gap Junction
Aids in cell-cell communication like in cardiac muscle or smooth muscle
Tight Junction
No space between cells (epithelium). Called septate junctions in invertebrates.
Anchoring Junctions
Attaches cell to cell or cell to extracellular matrix
type of anchoring junction that attaches the cell to another cell
type of anchoring junction that attaches a cell to the matrix. Aids in cell finding their way through the matrix.
type of anchoring junction that temporarily attaches a cell to another cell and tells the cell where to go.
Goes down a concentration gradient, doesn't require energy, size matters, charge matters and is not saturatable
completely random thermal energy
Fick's Law
J=(DxAxdeltaC)/X where J=Net flux, D=diffusion constant that is related to the molecule, A=Area, C=Change in concentration, and X=diffusion difference
Facilitated diffusion
Still passive, but requires a transport molecule, thus solutes move faster than simple diffusion and occurs to equilibrium and are saturatable
Electrochemical Equilibrium
Charges are concentrated alongside the membrane, but the extracellular fluid is more neutral
competition for the active site
carriers are specific to the molecule--> prefer glucose to galactose
Protein channels
1. Form tubes through membrane
2. Selective for ions based on size and charge
3. Channels don't saturate, but they can be turned off via electrical signals
Active Transport
Requires Energy (ATP) to pump ions out against a concentration gradient
Catalyzes a reaction, saturatable, reversible, specific.
LeChatlier's Principle
If you increase substrate, enzyme activity will increase until saturation.
LDH + Pyruvate --> LDH + Lactate
Occurs in the presence of little O2. When there is a lot of pyruvate, Lactate is formed, when there is a lot of lactate, pyruvate is formed.
velocity properties of a reaction (reaction rate)
maximum velocity, fastest reaction rate
gives measure of enzyme affinity. Substrate concentration at half of Vmax. Inverse relationship between Km and enzyme affinity --> Low Km equals high enzyme affinity
Reaction Rate determinants
Temperature and pH
Modulators of the enzyme
Allosteric, covalent, competitive, antagonist
Allosteric inhibitor
Binds to another place other than the active site on the enzyme and changes the shape of the enzyme so that it reduces its activity
Covalent modulation
phosphorylation of the enzyme
Competitive inhibitors
Bind to the active site on the enzyme and prevent the substrate from binding
Block the active site
related form of enzyme, differ by one amino acid, maintained by natural selection. Can make a protein not function, function differently, or function better. EX: LDH, Cytochrome P450, found in theliver, lungs, kidneys and each have a different function
Oxidation reduction reactions
Gain or loss of electrons. "Transfer of electrons to O2 and H+" Gain of e-. Ex: oxidase, dehydrogenase, reductase
hydrolysis and dehydration reactions
adding water to make a larger molecule or loosing water to make a larger molecule. Synthetase for dehydration along with reactions themselves. Hydrolysis = hydrolase, lipase, and protease
transfer of chemical group
1. Exchange +,- reaction, transfer of a phosphate group
2. additions (methyl, amino)
3. subtraction
Examples: transaminos, kinase
joining two substrates together, requires ATP energy Example: Ligase
Regulation of Metabolic pathways
1. Control the concentration of Enzymes
2. Produce Allosteric and Covalent modulation
3. Isozymes
4. Regulation of ATP/ADP ratio
ATP equation
ADP + Pi + energy --->ADP*Pi =ATP
Glycolysis equation
C6H12O6 + 6 O2 --> 6 CO2 + 6 H2O + heat + 38 ATP
converts fructose 6 phosphate to fructose 1, 6 diphosphate
Elements that allosterically modulate glycolysis
Citrate decreases catalytic activity AMP increases catalytic activity 100 fold
Pyruvate dehydrogenase
Allosteric inhibitor of glycolysis. ATP, Acetyl CoA, and NADH all inhibit this molecule in the presence of fatty acids in order to save pyruvate for gluconeogenesis.