Term
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Definition
| Every day humans turn over what percentage of protein and what tissue mainly |
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Term
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Definition
| enzyme that is secreted in the stomach for protein degradation |
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Term
1. trypsin 2. chymotrypsin 3. elastase 4. carboxypeptidases A and B |
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Definition
| 4 pancreatic enzymes released into the intestine for protein degradation |
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Term
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Definition
| enzymes secreted from intestinal mucosa or are used in the cells of the intestinal mucosa to degrate proteins |
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Term
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Definition
| is self activating in the presence of stomach acid |
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Term
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Definition
| is activated by enteropeptidase, and in turn, activates other pancreatic zymogens |
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Definition
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Definition
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Definition
| cleaves Phs, Tyr, Glu, Asp- aromatic or acidic AAs |
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Term
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Definition
| cleave amino acids at lysine or arginines |
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Term
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Definition
| favors cleaving Amino acids at hydrophobic residues, Phe, Tyr, Trp, Leu |
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Term
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Definition
| favors cleaving AAs at small side chains, alanine, glycine, and serine |
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Term
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Definition
| perferentially releases hydrophobic amino acids at the C teminal end |
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Term
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Definition
| releases basic amino acids at the C terminal, arginine and lysin |
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Term
| Na+ dependent carrier-mediated transport |
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Definition
| amino acids and dipeptides are absorbed into the intestinal cell by |
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Term
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Definition
| Na gradient created by this pump in the basolateral membrane in the intestinal endothelium, creates a concentration gradient to power amino acid absorbtion |
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Term
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Definition
| to leave the enterocyte, amino acids are carried down a concentration gradient by a |
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Term
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Definition
| inability of renal and intestinal epitheliat cells to absorb neutral amino acids |
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Term
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Definition
| impaired renal reabsorption causes |
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Term
| aromatic or hydrophobic side chains |
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Definition
| In Hartnup disease Amino acids with these features are inhibited |
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Definition
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| from mucosal lining, and digestive enzymes |
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Definition
| The endogenous proteins that are also degraded in the intestine |
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Term
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Definition
| contains 2 nitrogen and 1 carbon, none toxic, synthesize by the liver |
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Term
| normal input, increased output |
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Definition
| metabolic stress, illness, wasting - what is the nitrogen balence |
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Term
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Definition
| fasting, inadequate protein intake, lack of an essential amino acid - nitrogen balence |
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Term
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Definition
| causes muscle break down and thus increased urea synthesis, due to the fact gluconeogenesis is linked to urea synthesis |
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Term
| greater breakdown of amino acids |
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Definition
| burns, illness, glucocorticoids and epinephine, and sepsis causes |
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Term
| increased input, normal turnover and output |
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Definition
| happens to nitrogen balence in cases of growth, pregnancy, lactation, and recovery from metabolic stress |
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Term
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Definition
| requires primarily muscle work rather than dietary supplementation |
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Definition
| recommended daily allowance for males |
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Definition
| recommended daily allowance for females |
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Term
| recommended daily allowance |
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Definition
| these values are two standard deviations above mean requirements and cover nearly all healthy individuals |
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Term
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Definition
| individuals with low caloric intakes require a higher % of total calories as |
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| Still need the same amount of protein |
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Definition
| in older people, thier average energy utilization decreases, how does the requirements of protein change? |
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Term
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Definition
| catalyze NH3+ group transfer |
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Term
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Definition
| an amino group is transferred from an amino acid to an acceptor... |
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Term
| new amino acid and a new a-ketoacid |
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Definition
| products of an aminotransferase reaction |
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Term
| alanine aminotransferase (ALT) |
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Definition
| provides pyruvate for gluconeogenesis. alanine and a-ketoglutarate -> pyruvate and glutamate |
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Term
| aspartate aminotransferase (AST) |
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Definition
| reactions primarily runs in reverse, aspartate + a-ketoglutarate -> oxaloacetate + glutamate |
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Term
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Definition
| are the amino acid group donors of nitrogen for urea synthesis |
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Term
| alanine aminotransferas and aspartate aminotransferase |
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Definition
| high levels in plasma indicate liver damage |
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Term
1. histidine 2. lysine 3. proline 4. serine 5. threonine |
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Definition
| aminotransferases do not exist for what 5 amino acids |
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Term
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Definition
| central to the movement of amino groups between amino acids |
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Term
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Definition
| all aminotransferases utilize this as a cofactor for catalysis |
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Term
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Definition
| related chemical form of pyridoxal phosphate that also has vitamin activity |
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Term
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Definition
| high protein diets increase requirements for this vitamin |
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Term
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Definition
| accepts an amino group, donate it to another molecule, involves a schiff base intermediate |
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Definition
| labilizes the a bond on the amino acid structure |
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Term
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Definition
| labilizes the b bond on amino acid structure |
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Term
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Definition
| labilizes the c bond on amino acids |
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Term
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Definition
| mitochondrial enzyme, main pathway involved in creation of ammonium ions, oxidative deamination, hydrogen atoms transfered to NAD+, reversible |
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Term
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Definition
| used for glutamate synthesis and is the major physiological mechanism for incorporating NH4+ into organic molecules |
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Term
1. transaminase 2. glutamate dehydrogenase |
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Definition
| permits a-ketoglutarate to collect nitrogen from other amino acids and then release ammonia for urea synthesis |
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Term
| Serine enzyme- serine dehydratase |
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Definition
| forms pyruvate after a removal of water, creating unstable imino group follwed by water addition and loss of NH4+ |
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Term
| Threonine - enzyme threonine dehydratase |
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Definition
| forms a-ketobutyrate, dehydrated, unstable imino group, hydration and NH4+ release |
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Definition
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Term
| glutaminase and asparaginase |
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Definition
| these enzymes deamidate rather than deaminate |
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Term
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Definition
| particulary important in the kidney where NH4+ is used to buffer the urine |
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