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105 Cards in this Set
- Front
- Back
Sources of Thiamin |
Pork, Legumes, Whole fortified enriched grains, sunflower seeds |
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Can Thiamin be effected/destroyed by any factors |
Destroyed by heat and alkaline pH |
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What form is Thiamin found in animals foods? |
Thiamin Diphosphate aka Thiamin pyrophosphate |
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Where is FREE Thiamin absorbed? |
absorbed in the jejunum and ileum |
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How is the Thiamin Diphosphate converted to its free form |
intestinal phosphatase removes the phosphates Thiamin pyrophsophokinase |
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What are the factors that destroy Thiamin? |
Thiaminases (raw fish) Polyhydroxyphenols (tea, coffee, blueberries, brussell sprouts) These destroy the Thiamin ring, prevented in the presence of Vitamin C and citric acid Alcohol also inhibits absorption |
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Absorbed Thiamin is taken up where... |
in the liver phosphorylated to TDP |
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What is the percentages of TDP VS TTP in the body? |
80% TDP 10% as TTP |
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Is Thiamin carrier mediated? |
Yes |
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What is the enzyme that converts Thiamin to it's coenzyme form TDP |
thiamin pyrophosphokinase |
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What is the antithiamin factor that comes from raw fish? How can it be destroyed? |
Thiaminases By heat |
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What is the antithiamin factor that comes from coffee, tea, blueberries, brussel sprouts? How can it be destroyed? |
Polyhydroxyphenols they are stable in heat but can be inhibited by Vitamin C and citric acid |
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Does alcohol effect Thiamin? |
Inhibited by alcohol |
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What complexes is Thiamin's coenzyme TPP involved in? |
"Dehydrogenases" 1. Pyruvate dehydrogenase comlex 2. alpha ketoglutarate dehydrogenase complex 3. BCA dehydrogenase complex |
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What does inhibition of Thiamin or it's coenzymes? |
prevents synthesis of ATP and acetyl CoA needed for synthesis of fatty acids, cholesterol, and allows for accumulation of lactate, pyruvate, and alpha keto gluturate |
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Pyruvate dehydrogenase complex overall reaction |
Pyruvate + NAD+ + Coa--> Acetyl Coa +NADH + H+ + Co2 |
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Pyruvate Dehydrogenase complex, is _________ dependent. How? |
TPP dependent C2 of the Thiazole ring forms a carbonion making it open to a neuleophilic attack from pyruvate alpha keto glutarate and other alpha ketoacids |
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What is the function of the Pentose Phosphate Pathway? |
Synthesis of Pentose sugars and NADPH |
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Transketolase needs the enzyme... |
TPP for the Phosphate Pentose Pathway |
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What is Thiamin (TPP) non coenzyme role? |
Nerve conduction |
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RDA for Thiamin is based on... |
1. Urinary excretion 2. RBC transketolase activity 3. Thiamin intake data |
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What is the difference between Dry and Wet Beriberi |
Dry is nerve Wet is the heart |
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What is the disease associated with the deficiency of Thiamin? |
BeriBeri |
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What is the structure of Riboflavin? |
flavin molecule (isoalloxazine ring) with ribotol side chain |
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What are the two coenzymes of Riboflavin? |
FMN AND FAD |
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What are the food sources of Riboflavin? |
Milk and milk products, eggs, meat, legumes, liver |
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Is Riboflavin effected by light/heat/acid/alkaline? |
Destroyed by sunlight Resistant to heat, oxidation, and acid |
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Riboflavin must be in _______ form for absorption |
Free form only |
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Where is Riboflavin absorbed? |
Small intestine |
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Is Riboflavin carrier mediated? *** In large amounts? |
Yes saturable energy dependent In large amounts passive absorption |
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Does alcohol effect Riboflavin? |
Alcohol inhibits |
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What substance stimulates absorption of Riboflavin? |
Bile |
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In the liver Riboflavin..... |
is converted to FMN and FAD after absorption |
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What enzymes convert Riboflavin in the liver? |
Flavokinase and FAD synthetase |
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Free riboflavin is absorbed into..... by.... |
Tissues by riboflavin binding proteins |
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Where are the greatest sources of free Riboflavin that have been absorbed into the tissues found? |
Liver, kidney, and heart |
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Within the cells of tissue Riboflavin is.... |
converted to FMN and FAD |
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When bound to it's apoenzyme Riboflavin is.... |
a Flavoprotein |
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What is the function of Riboflavin's coenzyme? |
FMN and FAD Oxidation/reduction reactions |
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Specifically how does FMN and FAD participate in oxidation/reduction reactions? |
The Isoalloxazine ring accepts/donates a pair of H one electron at a time--> FMNH2 and FADH2 |
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What are the functions of flavoproteins? |
1. Electron Transport Chain 2. Vit. B6 metabolism 3. Oxidative decarboxylation of pyruvate and alpha keto glutarate 4. B oxidation, acyl Coa Dehydrogenase 5. Synthesis of THF, cofactor form of folate |
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The RDA of Riboflavin is based on |
1. Urinary excretion 2. Relation of diet to clinical symptoms of deficiency 3. RBC glutathione reductase |
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What is the disease of deficiency of Riboflavin? |
Ariboflavinosis (no clear characterization) Maybe be seen in excessive alcohol |
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How do you test the nutriture of Riboflavin? |
Measure activity of erythrocyte FAD- dependent glutathione reductase with and without FAD addition AC greater than 1.4 = deficiency |
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What is the enzyme that used to assess both the RDA and the state of nutriture for riboflavin? |
Erythrocyte glutathione reductase (FAD dependent) |
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What is the name given tothe protein or enzymes that bind FMN and FAD?
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flavoprotein? |
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What are the two forms of Niacin |
Nicotinic Acid and Nicotinamide |
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What are the food sources of Niacin? |
Fish and meats Enriched cereals and grains Legumes and seeds |
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is Niacin effected by heat/acid/alkaline/light? |
Minimal loss with cooking and storage |
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How is Niacin found in food primarily? |
Nicotinamide, nicotinic acid, NAD+, NADP+ |
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What is the relationship between corn and Niacin? |
only 10% of niacin available in corn because of small peptides called niacinogens |
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Other than food Niacin can also be found.. |
Synthesized in the liver from tryptophan |
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What % of tryptophan is metabolized to niacin? |
3% |
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Where are free nicotinamide and nicotinic acid absorbed? |
small intestine |
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Do nicotinamide and nicotinic acid need a carrier? |
Yes, saturable carrier |
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In oxidation which dominates, NAD+ or NADH? |
NAD+ |
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In reduction which dominates, NADP+ or NADPH? |
NADPH |
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What is the coenzyme role of Niacin? |
Dehydrogenases require NAD and NADP as coenzymes; tightly bound to apoenzyme. They are H+ donors and acceptors |
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NADH role |
formed from NAD, transfers its electrons picked up from metabolic intermediates to the ETC--> ATP |
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NADPH role |
reducing agent in biosynthesis reactions (fatty acids, cholesterol, steroid hormones) |
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NAD role... required for catabolism of.... |
Vitamin B6 |
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Non redox role of Niacin... |
DNA function and calcium signaling |
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The RDA for Niacin is based on.. |
Human depletion and repletion studies Studies with primary urinary metabolites |
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What is the deficiency disease of Niacin? |
Pellegra, 4 D's |
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Deficiency of Niacin from medications.. |
Isonaizid (tuberculosis) inhibits niacin synthesis Mercaptopurine (cancer)- inhibit NAD phosphorylase |
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Does alcohol inhibit Niacin |
no |
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Does Niacin have toxicity symptoms? |
Yes, large doses to treat hypercholesterolemia; niacin appears to block VLDL production (not a bad thing) Pharmacological doses--> decreased cholesterol, triglycerides and LDL, increased HDL |
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What is the UL of Niacin? |
35 mg |
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How do you assess the nutriture of Niacin? |
Measurement of urinary metabolite levels RBC NAD and NADP concentrations Plasma 2-pyridine drops with low niacin intake; indicator |
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What is the structure of pantothentic acid? |
B-alanine and pantoic acid joined by a peptide bond part of coenzyme A |
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What are the sources of pantothenic acid? |
Almost all plant and animal foods Liver kidneys, yeast, egg yolk, broccli |
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Is pantothenic acid destroyed be heat/light/acid/alkaline? |
Easily destroyed by heating and freezing Destroyed by acidic and alkaline solutions |
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Pantothenic acid is 85% of the time found as _______ in food |
Coenzyme A |
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Where is Pantothenic Acid digested? |
GI tract where it is converted to free pantothenic acid |
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Where is pantothenic acid absorbed? |
Jejunum |
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Does pantothenic acid require a carrier? High concentration vs low concentration |
Passive at high Carrier dependent at low (Sodium Dependent Multivitamin Transporter) |
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SMVT is shared with .... high doses of pantothenic acid.... |
SMVT is shared with biotin and lipoic acid. High doses of pantothenic acid interfere with biotin absorption in the intestine and the tissue levels. |
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How is Pantothenic Acid transported? |
Red blood cells |
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Where is pantothenic acid converted to Coenzyme A? |
inside of the cells |
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Pantothenic acid functions as a component of.... |
1. Coenzyme A 2. 4'-phosphopantatheine |
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What is the structure of Coenzyme A? |
Phosphoantatheine and adenosine-3',5'-biphosphate |
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Coenzyme A forms _____ linkage with _______ of molecules; which ____________ |
Coenzyme A forms a thioester linkage with carboxylic acid of molecules which activates them |
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Coenzyme A can transfer the acyl groups (2-13 carbons) of.... |
Acetic acid Propionic acid methylmalonic acid succinic acid |
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Coenzyme A is part of the __________ complex |
Pyruvate dehydrogenase Introduces acetate for oxidation Joins thiamin, riboflavin, and niacin in decarboxylation of pyruvate, alpha ketogluturate (TCA) and succinate (TCA) |
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Coneyzme A transfers aceytl groups, which involves it in synthesis of... |
1. Cholesterol (Acetyl CoA+ Acetoacetyl Coa) 2. Fatty acids (Acetyl CoA + CO2) 3. Bile Salts 4. Ketone bodies 5. Steroid hormones |
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Conenzyme A in acetylation of Nutrients: Sugars and Proteins |
A. Post transitional modifications of proteins B. Choline --> acteylcholine C. Acetylated sugars= cell surface molecules |
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Coenzyme A in fatty acid synthesis via Acyl Carrier Protein (ACP) |
ACP is part of Fatty Acid Synthase Complex SH group in 4'-phosphopantatheine of ACP bind and transfer acyl group (growing fatty acid) |
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RDA for Pantothenic Acid |
None establish |
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Deficiency of Pantothenic Acid |
Rare |
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Assessment of nutriture |
Urinary pantothenic acid levels reflect dietary intake as excreted intact |
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Raw egg whites block which vitamin? |
Biotin Because of the substance avidin which tightly binds biotin inhibiting absorption |
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What is the structure of Biotin? |
Ureido ring and thiophene ring with valeric acid side chain |
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Biotin sources |
Colonic bacteria Widespread in foods Beef, soybean, liver, (cooked) egg yolk, cereal, and legumes In food biotin covalently bound to protein or biotin linked to lysine (biocytin) |
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What is biocytin |
Biotin linked to lysine |
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Protein bound biotin is digested by... to.... |
Digested by Proteases into biotin and biocytin |
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Biocytin is digested by... |
Biotinidase in intestine and plasma |
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Free biotin is absorbed... |
proximal small intesting (jejunum mostly) |
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Free biotin needs a carrier? |
Yes, SMVT |
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Sharing a transporter, panothenic acid and biotin creates a problem b/c |
they have to compete and could inhibit eachother |
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Biotin's coenzyme role |
Metabolism of Carb, amino acids, and fatty acids -bound to 4 carboxylases |
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Attachment of biotin to a carboxylase requires... |
Holocarboxlase synthetase |
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What are the four carboxylases Biotin attaches to |
1. Pyruvate carboxylase 2. Propionyl CoA Carboxylase (catabolism of odd carbon fatty acids) 3. Acetyl CoA Carboxylase 4. B-methylcortonyl CoA carboxylase |
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Deficient in biotin--> |
urinary excretion of 3-hydroxyisovaleric acid, 3-HIA |
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Biotin non coenzyme role |
Biotinylation of hisones--> unpacking of DNA translation of some RNAs |
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Assessment of Nutriture |
urinary biotin excretion increased urinary 3-HIA excretion=deficiency |