Animal Physiology Test 1 Introduction

Front 1

Homeostasis

Back 1

regulation of your internal environment to face the changing external environment

Front 2

Conformity

Back 2

Opposite of homeostasis. Allows parameter to change with external environment

Front 3

Membrane function

Back 3

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

Front 4

Two types of membrane proteins

Back 4

peripheral and integral

Front 5

What is a CHO group used for within the membrane?

Back 5

signaling and immune signals

Front 6

desaturase

Back 6

Aids in the fluidity of the membrane during times of colder temperature by unsaturation of the lipid molecules

Front 7

Four types of tissue

Back 7

Connective, Muscle, Nervous, Epithelial

Front 8

Two types of extracellular fluid

Back 8

Plasma, interstitial fluid

Front 9

Three types of Junctions

Back 9

Gap Junction, Tight junction, Anchoring junction

Front 10

Gap Junction

Back 10

Aids in cell-cell communication like in cardiac muscle or smooth muscle

Front 11

Tight Junction

Back 11

No space between cells (epithelium). Called septate junctions in invertebrates.

Front 12

Anchoring Junctions

Back 12

Attaches cell to cell or cell to extracellular matrix

Front 13

cadherins

Back 13

type of anchoring junction that attaches the cell to another cell

Front 14

integrins

Back 14

type of anchoring junction that attaches a cell to the matrix. Aids in cell finding their way through the matrix.

Front 15

selectins

Back 15

type of anchoring junction that temporarily attaches a cell to another cell and tells the cell where to go.

Front 16

Diffusion

Back 16

Goes down a concentration gradient, doesn't require energy, size matters, charge matters and is not saturatable

Front 17

entropy

Back 17

completely random thermal energy

Front 18

Fick's Law

Back 18

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

Front 19

Facilitated diffusion

Back 19

Still passive, but requires a transport molecule, thus solutes move faster than simple diffusion and occurs to equilibrium and are saturatable

Front 20

Electrochemical Equilibrium

Back 20

Charges are concentrated alongside the membrane, but the extracellular fluid is more neutral

Front 21

competition for the active site

Back 21

carriers are specific to the molecule--> prefer glucose to galactose

Front 22

Protein channels

Back 22

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

Front 23

Active Transport

Back 23

Requires Energy (ATP) to pump ions out against a concentration gradient

Front 24

Enzyme

Back 24

Catalyzes a reaction, saturatable, reversible, specific.

Front 25

LeChatlier's Principle

Back 25

If you increase substrate, enzyme activity will increase until saturation.

Front 26

E+S--->

Back 26

ES--->EP--->E+P

Front 27

LDH

Back 27

LDH + Pyruvate --> LDH + Lactate
NADH + NAD+
---------->
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.

Front 28

Kinetics

Back 28

velocity properties of a reaction (reaction rate)

Front 29

Vmax

Back 29

maximum velocity, fastest reaction rate

Front 30

Km

Back 30

gives measure of enzyme affinity. Substrate concentration at half of Vmax. Inverse relationship between Km and enzyme affinity --> Low Km equals high enzyme affinity

Front 31

Reaction Rate determinants

Back 31

Temperature and pH

Front 32

Modulators of the enzyme

Back 32

Allosteric, covalent, competitive, antagonist

Front 33

Allosteric inhibitor

Back 33

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

Front 34

Covalent modulation

Back 34

phosphorylation of the enzyme

Front 35

Competitive inhibitors

Back 35

Bind to the active site on the enzyme and prevent the substrate from binding

Front 36

Antagonist

Back 36

Block the active site

Front 37

Isozyme

Back 37

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

Front 38

Oxidation reduction reactions

Back 38

Gain or loss of electrons. "Transfer of electrons to O2 and H+" Gain of e-. Ex: oxidase, dehydrogenase, reductase

Front 39

hydrolysis and dehydration reactions

Back 39

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

Front 40

transfer of chemical group

Back 40

1. Exchange +,- reaction, transfer of a phosphate group
2. additions (methyl, amino)
3. subtraction
Examples: transaminos, kinase

Front 41

ligation

Back 41

joining two substrates together, requires ATP energy Example: Ligase

Front 42

Regulation of Metabolic pathways

Back 42

1. Control the concentration of Enzymes
2. Produce Allosteric and Covalent modulation
3. Isozymes
4. Regulation of ATP/ADP ratio

Front 43

ATP equation

Back 43

ADP + Pi + energy --->ADP*Pi =ATP

Front 44

Glycolysis equation

Back 44

C6H12O6 + 6 O2 --> 6 CO2 + 6 H2O + heat + 38 ATP

Front 45

phosphofructokinase

Back 45

converts fructose 6 phosphate to fructose 1, 6 diphosphate

Front 46

Elements that allosterically modulate glycolysis

Back 46

Citrate decreases catalytic activity AMP increases catalytic activity 100 fold

Front 47

Pyruvate dehydrogenase

Back 47

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.