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106 Cards in this Set
- Front
- Back
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What are isotopes?
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same physical properties, different masses, same # of protons, different # of neutrons
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What is the atomic #?
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# of protons in an atom
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What is atomic mass?
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# of protons + # of neutrons
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What elements are needed in the body in abundance?
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H, O, Ca, C, N, P, Mg, Na, Cl, S, K, Fe (can be considered trace also)
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What is the dissociation constant for strong acids?
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large
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which amino acid is not optically active?
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glycine
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what are the nonpolar amino acids?
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glycine, alanine, valine, leucine, isoleucine, methionine, proline, phenylalanine, and tryptophan
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what amino acid is actually an a-imino acid?
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proline
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what three amino acids can be phosphorylated by kinases?
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threonine, serine, and tyrosine
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what amino acids contain amide derivatives of a carboxylic acid?
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asparagine (asn) and glutamine (gln)
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what are the uncharged polar amino acids?
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serine, tyrosine, threonine, glutamine, asparagine
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what amino acids are deprotonated at physiological pH?
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aspartate (asp) and glutamate (glu), have carboxylic acid side chains
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what amino acids are protonated at physiological pH?
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lysine and arginine, found in histones
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what amino acid is often used in catalysis because it can be protonated or deprotonated?
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histidine, pK value is within physiological range
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what amino acid can be oxidized to form disulfide bonds?
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cysteine
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what amino acid commonly occurs at protein bends?
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proline
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what causes alzheimers and transmissible spongiform encephalapathies?
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misfolded proteins which aggregate into amyloid fibrils
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what does SDS-PAGE do?
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separates proteins as a function of size
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what does isoelectric focusing do?
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separates proteins and amino acids by charge through a pH gradient. negative = anode. positive = cathode
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what do CO, NO, and H2S do to hemoglobin?
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bind iron atoms in Hb tightly and irreversibly
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what type of curve does binding of O2 to myoglobin make?
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hyperbolic
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what does the hill equation determine?
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cooperativity
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what does sickle cell anemia result from?
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a change of a glutamic acid residue to a valine
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what is the result of competitive inhibition?
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increase KM, no effect on Vmax, same y intercept on LB since Vmax is unchanged, X intercept will be less -
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what is the result of noncompetitive inhibition?
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no effect on KM, decrease Vmax, y axis will be higher (1/Vmax) and x axis will stay the same
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what happens in mixed inhibition?
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KM will increase, Vmax will decrease, higher on y, less negative on X
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what happens in uncompetitive inhibition?
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Vmax and KM will both decrease (binds only to the ES complex)
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what is the carbon called that becomes the chiral center upon cyclization?
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anomeric carbon
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what are enzymes that catalyze the hydrolysis of glycocytic bonds?
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glycosidases
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what are reducing sugars?
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sugars with unbound anomeric carbons, easily oxidized
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what is glucosaria?
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glucose in the urine
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what are amino sugars?
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sugars with one or more OH group replaced by an amino group
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what acetylated amino sugars are found in bacteria?
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N-acetylglucosamine and N-acetylmuramic acid that make up peptidoglycan
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what are the monos of sucrose?
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glucose and fructose
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what are the monos of lactose?
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glucose and galactose
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what are the monos of maltose
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glucose and glucose
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what is starch?
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food reserve in plants, nutrient in animals
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what is starch composed of?
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amylopectin and a-amylose
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what is a-amylose?
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thousands of glucose connected by a (1-->4) bonds
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what is amylopectin?
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same as a-amylose though also contains branching of a(1-->6) variety
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what bonds do a-amylase in saliva breakdown in starch?
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a(1-->4) unless adjacent to branch points
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what does pancreatic a-amylase breakdown starch into?
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maltose, trisaccharide maltotriose, and dextrins that contain a(1-->6)
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what does dextrinase do?
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hydrolyzes a(1-->6) branches
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what does I cell disease result from?
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inability to send lysomomal enzymes to the lysosome because they do not get marked with mannose-6-phosphate
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what does lysozyme do?
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cleaves B-1,4 linkages between NAG and NAM
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what converts procollagen into collagen?
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procollagen proteases that cleave the N and C terminal ends
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what does lysyl oxidase do?
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modifies lysine and hydoxylysine residues in the ECM to form aldehyde cross links (lysine --> allysine)
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what synthesizes hydroxyproline and what does it require?
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prolyl hydroxylase..requires vitamin C
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what does prolyl hydroxylase require?
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vitamin C, oxygen, proline, a-ketoglutarate, and Fe
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proline + O2 + a ketoglutarate -->
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succinate + hydroxyproline + CO2
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what is vitamin C required for in the prolyl hydroxylase reaction?
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regenerates the reduced form of Fe that is required for this reaction
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what causes lathryism?
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inactive lysyl oxidase activity, serious abnormalities in bones, joints, and blood vessels
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what is fibronectin necessary for?
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cell adhesion
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describe hyaluronate.
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major component of ground substance. is only glycosaminoglycan that is not sulfated. longest of the glycosaminoglycans
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what is heparin?
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it is an anticoagulant that is not found in connective tissue but is present in intracellular granules of mast cells, can be given to prevent excessive clotting
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what prevents glucose from leaving the cell?
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glucose is phosphorylated into G-6-P by hexokinase
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what enzyme changes a 6C to a 3C in glycolysis?
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aldolase
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what do the "priming rxns" of glycolysis do?
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they use 2 ATP and form glyceraldehyde-3- phosphate
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what enzyme is inhibited by fluoride? what does it require?
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enolase, Mg2+
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what do the last rxns of glycolysis do?
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produce 4 ATP and do one oxidation reaction to produce NADH
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what produces lactate from pyruvate?
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lactate dehydrogenase
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what is the sole purpose of fermentation?
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to regenerate NAD+ for the glyceraldehyde-3-phosphate dehydrogenase rxn
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what does PFK do?
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converts F-6-P to F-1,6-BP while using ATP
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what prosthetic groups does pyruvate dehydrogenase require?
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thiamin, niacin, riboflavin, pantothenic acid, and lipoic acid
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what enzyme is similar in prosthetic group an rxn to pryuvate dehydrogenase?
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a-ketoglutarate dehydrogenase. a-ketoglutarate -->succinyl CoA
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which enzyme of TCA is also part of e- transport chain?
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succinate dehydrogenase. succinate --> fumarate which produces FADH2
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what inhibits pyruvate dehydrogenase?
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NADH, acetyl CoA, and phosphorylation (which happens because ATP is high in the cell and kinase uses it for energy)
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what makes oxaloacetate?
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pyruvate carboxylase
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what does cyanide do?
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inhibits electron transport chain
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what does oxidative phosphorylation involve?
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transfer or electrons between components that are sequentially stronger oxidants
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what coenzymes does Complex I have?
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FMN (electron carrier protein) and FeS
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what is a cytochrome?
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a heme prosthetic group containing protein that does not hold or transfer O2. The Fe atom transfers between a ferric (+2) and a ferrou (+3) state.
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what element does complex IV use?
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copper
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what is the F0 portion of atp synthase?
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transmembrane proton channel
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what is the F1 portion of atp synthase?
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synthesizes ATP
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what is an example of an uncoupler?
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dinitrophenol
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what targets proteins to the membrane?
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lipid linked proteins
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what defines a primary transporter?
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ATP hydrolysis is the direct source of energy to pump substances across a membrane
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what are P type transporters?
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a type of primary transporter where the ATP hydrolysis results in the transporter becoming phosphorylated
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what are ATP binding cassettes?
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a type of primary transporter where the ATP hydrolysis does not result in the transporter becoming phosphorylated
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what is an example of a secondary transporter?
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Na-glucose symporter. Energy is used to create Na+ gradient. This energy is then used to transport glucose into the cell with Na coming down its gradient
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what are voltage gated channels classified as?
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facilitated diffusion
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what is transported into the mitochondria when NADH is created?
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electrons, NOT NADH!!
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what are the two main types of transporter to get electrons from NADH into the mitochondria?
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G3P shuttle (e- transferred to FADH2) and malate aspartate shuttle
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what GLUT transporter is expressed in brain and erythrocytes?
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GLUT 1 and GLUT 3
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what GLUT transporter is expressed in the liver?
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GLUT 2, very high Km
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what GLUT transporter is expressed in muscle and fat cells?
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GLUT 4
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what is GLUT 5
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fructose transporter
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what are the predominant linkages in glycogen and what are the branching point linkages?
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a-1,4 and a-1,6
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what cleaves glycogen a-1,4 linkages?
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glycogen phosphorylase
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what is required for degradation of a-1,6 linkages?
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transferase and debranching
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what does the PPP produce from G-6-P?
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ribose and NADH
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what enzyme does the liver use to release glucose?
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glucose-6-phosphatase
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what type of glucose does glycogen phosphorylase release from glycogen?
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glucose-1-phosphate
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what does glycogen phosphorylase require?
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pyridoxal phosphate (vitamin B6)
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what form of glycogen phosphorylase does AMP activate?
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phosphorylase b, active form, high AMP = low ATP
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what amino acids are not gluconeogenic?
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leucine and lysine
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what 4 enzymes are used in the gluconeogenic pathway that were not used in glycolysis?
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pyruvate carboxylase (uses ATP), phosphoenolpyruvate carboxykinase (uses GTP), fructose -1,6-bisphosphatase, and glucose-6-phosphatase
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where does glycerol from triacylglycerol breakdown enter the gluconeogenic cycle?
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as DHAP
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how does the cori cycle work?
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lactate produced in the muscle is released into the blood where the liver takes it up and converts it to glucose
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what does F-2,6-BP activate?
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glycolysis, activated by insulin
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what synthesizes F-2,6-BP?
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phosphofructokinase 2
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what hydrolyzes F-2,6-BP?
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fructose bisphosphate 2
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what does the pentose phosphate pathway make?
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NADPH, ribose sugars (pentoses), fructose-6-P, glyceraldehyde-3-phosphate
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what does glucose-6-phosphate dehydrogenase do?
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catalyzes the formation of NADPH from glucose-6-phsophate
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what is lactose intolerance caused by?
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lack of lactase
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