• VITAMINS • Group of organic nutrients • Small quantities • Not synthesised in the body • Supplied in the form of diet • Maintainance

of normal metabolic activity Exception:  Vitamin D made in skin after exporsure to sunlight  Niacin formed from essential aminoacid tryptohphan • Fat Soluble • A, D, E and K • Fat soluble • Apolar, hydrophobic • Isoprene derivatives • Bile salts and fats essential for their absorption • Stored in liver Vitamin A D2 D3 E K • • • • • • • •

Chemical name Retinol Ergocalciferol (in plants) Cholecalciferol (in exposed skin) Tocopherol Phylloquinone Not excreted in urine VITAMIN A Retinoids Retinol (preformed vitamin A)  Most potent form  Can be synthesized from retinal Retinal  Can be converted to retinoic acid Retinoic acid Dietary Sources Retinol activity equivalent (RAE) 1 RAE = 12 µg beta-carotene & 1µg retinol Preformed vitamin A (retinol): Organ meats, liver, fatty fish, dairy products Provitamin A (carotenes) : Yellow, orange, red fruits/veg, leafy greens

• •

. retinal of rhodopsin is in the 11-cis form (c). • In the dark.• Precursor (β-carotene) 2 molecules of Vitamin A1 and derivatives. • Retinal + protein opsin to form rhodopsin (not shown in above structure) a visual pigment widespread in nature.

c. Rhodopsin + light ------→ Retinal + opsin (found in rod cells) (absorbs light. • Inadequate amounts of retinal to re-form rhodopsin • Night vision becomes difficult • Functions (continued) • Maintaining the integrity of the mucous membrane and healthy skin. This transformation in the rod cell of the vertebrate retina sends an electrical signal to the brain that is the basis of visual transduction Functions of Vitamin A Vision: part of visual pigment rhodopsin. Infections of urinary and respiratory tract. Changes in GI tract lining. Drying and hardening of the cornea--“xeropthalmia”: Mild-xerosis. causing diarrhea. loss of appetite. • Vitamin A deficiency 1. • Needed for manufacture of RBC. needed especially to see in dim light. Impaired night vision (night blindness). Bitot spot Severe – keratomalacia (total blindness) b. • Role in reproduction and immune reactions.• • • When a rhodopsin molecule is excited by visible light. causing: a. and mucous membranes fail to secrete mucus. 2. changes shape and is bleached) • Night Blindness: slow recovery of vision after flash of bright light at night. Drying and hardening of salivary glands. d. Dried skin. the 11-cis-retinal undergoes a series of photochemical reactions that convert it to all-trans-retinal (e). susceptible to infection. • . forcing a change in the shape of the entire rhodopsin molecule. • Essential for bone growth and bone remodeling (osteoclasts contain lysosomes).

3. • Vitamin D (Cholecalciferol) • sources • Rich sources: Liver and Viscera of fish • Good sources: Eggs and butter • Poor sources: Milk • Cheapest source: Sunlight. anemia • Bitot spot-buildup of keratin debris located superficially in the conjunctiva. . triangular or irregular in shape. Abnormal bone growth 4. • softening and necrosis of the cornea associated with vitamin A deficiency. and red. Fine cracks may appear on the skin • Keratomalacia is an eye disorder that leads to a dry cornea. Skin (epithelial cells) and hair follicles plugged with keratin (follicular hyperkeratosis). itchy. which are oval. Symptoms: The skin is dry. • Xerosis is an abnormal dryness of the skin or mucus membranes.e. scaly.

Blood: Decreased Ca and/or P Teeth: Slow eruption.• • • • • • • • • • • • • • • • • Vitamin D Deficiency Rickets (in children) Bone: Poor calcification and retarded growth. fish. enlargement of ends of long bones. deformities of ribs. where exposure to O2 is maximal. protects RBC and cells of lungs itself. chicken. – Vitamin E is also protective against strong oxidizing agents like ozone and nitrogen dioxide – air pollutants. bowed legs. deformities of spine. Osteomalacia (in adults) Bone: Softening of bones. liver. These cause peroxidation of cell membrane lipids. – One of the most important organs where vitamin E exerts its antioxidant effect in lungs. pain in lower back and pelvis. Cell membrane structure . cottonseed oil etc. Blood: Decreased Ca and/or P levels Involuntary twitching. beaded ribs. bone fracture. It protects vitamin A and polyunsaturated fatty acids from oxidation. Before and after (14 months) of vitamin D treatment Vitamin E (Tocopherol) sources Egg. tendency to decay. muscle spasms. meat. Antioxidant: compound that protects others from oxidation by being oxidize itself. not well formed. Functions Vitamin E acts as an “antioxidant”. corn oil. knock knees.

. causing membrane structure to break down. cabbage etc. alfa alfa.. Fair sources: Carrots and Potatoes Poor sources: Milk. spinach. Good soucres: Cauliflower. Polyunsaturated fatty acids in cell membranes are oxidized. meat and fish Made by intestinal bacteria Vitamin K is essential for synthesis of several proteins needed for blood coagulation or clotting. VITAMIN K (coagulating factor) Chemistry Two naturally occuring vitamin K Vitamin K1 (Phylloquinone) Vitamin K2 (Farnesoquinone) Menadione is the most important synthetic vitamin K-These lack long hydrocarbon chain-Hence soluble in water. Vitamin E deficiency rare in humans Vitamin E toxicity: not known in humans.• • • • • • • • • • • • • • • • • • Deficiency of Vitamin E: “Hemolysis”: Bursting of red blood cells.. Wheat germ etc. Soya bean. sources Best: Green leafy vegetables Eg.

Inositol • Mnemonic:The romans never painted pyramids before college Vitamin B1 B2 B3 B5 B6 Chemical name Thiamin Riboflavin Nicotinamide (niacin) Pantothenic acid Pyridoxine • Water soluble vitamins . X) Essential component of the phosphorylation process in photosynthesis Involved in electron transport chain and it involved in oxidative phosphorylation Required for the absorption of fat Acts as cofactor (to the enzyme carboxylase) for the carboxylation (addition of CO2) of glutamate residues Forms unusual amino acid α –carboxyglutamate Chelates calcium ions Process takes place in postsynthetic modification of calcium binding proteins Deficiency Leads to lowering of prothrombin level and increase clotting time of blood Prolongation of prothrombin time This may lead to hemorrhagic conditions Ascorbic acid (vitamin C) Vitamin B complex B1. B6. Folic acid.• • • • • • • • • • ↓ • • • • • Functions Catalyses the synthesis of prothrombin by the liver Reduces prothrombin time Regulates the synthesis of plasma clotting factors (II. B12 . VII. B2. Lipoic acid. Biotin. Niacin. Pantothenic acid. IX.

Fair sources: Grapes. tomatoes. guava. papaya. banana. ASCORBIC ACID Sources • • • • • Richest soucres: Amla (Indian goosebury). potatoes.B7 Biotin Folic acid-B9 Choline B12 C Cyanocobalamin Ascorbic acid • • • • • • • • • • Properties Water soluble Polar molecules Diverse chemical nature. freshly killed meat. raw cabbage. milk. green peppers. No similarity of chemical structure between them Easily absorbed They are not stored in body (except B12) They have threshold for urinary excretion Act as coenzymes of different enzyme catalysed reaction except ascorbic acid which itself act as an enzyme. fresh raw fish. green leafy vegetables. apple. cauliflower. Good sources: citrus fruits. Physiological functions Vitamin C is Sensitive to reversible oxidation-Powerful reducing agent Acts as antioxidant in solution Involved (acts as cofactors) in the conversion of • folic acid to folinic acid • Dopamine to norepinephrine . liver. jackfruit.

eggs. wheat germ and yeast • Good sources: Cereals. bone.. fish. In oxidative decarboxylation of α keto acids (Pyruvic acid and α ketoglutaric acid which are intermediates of carbohydrate metabolism) • • . oilseeds. • Deficiency • Scurvy-The signs of deficiency is entirely confined to supporting tissues of mesenchymal origin viz. nuts.sponginess. • Fair sources: Meat. pulses. • Involved in the metabolism of tyrosine. dentine.In phenyl alanine metabolism in the conversion of p-hydroxyphenyl pyruvic acid to homogentisic acid • Involved in the hydroxylation of steroids (In adrenal cortex) • Participates in hydroxylation of proline and lysine present in collagen. vegetables and fruits • Functions • Thiamine is essential for growth • It is essential for maintaining nerves in normal condition. tenderness and bleeding of gums • Anemia • Susceptibility to infections • General weakness VITAMIN B1 (Thiamine) • sources • Best: Rice polishings. milk. • It has got coenzyme activities Thiamine is converted to its active form TPP (Thiamine pyrophosphate)—by ATP dependent thiamine pyrophosphokinase which is present in brain and liver • Coenzyme function • Coenzyme:Thiamine pyrophosphate (TPP)--Used mainly as coenzyme in carbohydrate metabolism 1. Essential for normal regulation of the colloidal condition of intercellular substances including • Fibrils and collagen of connective tissue • Osteoid tissues • Dentine • Intercellular cement substance of the capillaries Required for the • Absorption of iron by reducing ferric form to ferrous form • Incorporation of plasma iron in ferritin. phenyl alanine and also in tryptophan. cartilage and connective tissue Characterised by failure in the formation and maintainance of intercellular materials which causes typical symptoms such as • Internal haemorrages • Loosening of the teeth • Poor healing of wounds • Swelling of long bones • Easy fracturability of bones • swelling.

carried temporarily on enzyme bound TPP. • It is also the coenzyme for transketolase. from a ketose donor to an aldose acceptor.• pyruvate dehydrogenase complex Pyruvic acid ---------------------------------→Acetyl CoA which enters citric acid cycle • • α-ketoglutarate dehydrogenase complex α Ketoglutaric acid -------------------------→Succinyl CoA (citric acid cycle) Carbohydrate Biosynthesis in Plants and Bacteria: Transketolase-catalyzed reactions of the Calvin cycle. in the pentose phosphate pathway (Hexose monophosphate shunt p • athway) General reaction catalyzed by transketolase: the transfer of a two-carbon group. .

key enzymes in fatty acid and amino acid oxidation. • VITAMIN B2 (Riboflavin) • sources • Widely distributed throughout plant and animal kingdoms.• Beriberi: Wet beriberi: • Oedema is the most prominent feature and developed rapidly in the legs. • Urine volume is diminished but there is no albuminuria. The subject needs stick to stand and walk and finally becomes bedridden because muscles become weak. liver. • The free riboflavin present in retina is converted by light to a compound involved in stimulation of the optic nerve. fish. heart. • • Coenzyme function Riboflavin fulfills its role in metabolism as the coenzymes by ATP-dependent flavin mononucleotide (FMN) : FMN is formed phosphorylation of riboflavin flavin adenine dinucleotide (FAD): FAD is synthesized by further reaction of FMN with ATP in which its AMP moiety is transferred to the FMN. Dry beriberi: • The essential feature is polyneuropathy. • Pulse is fast. face etc. . germinating wheat and barley. roots. • Fair sources: cereals. • Best: Anaerobic fermenting bacteria • Good sources: Milk. kidney. Flavin Coenzymes Are Electron Carriers in Oxidoreduction Reactions: These include the mitochondrial respiratory chain. • Functions • Involved in regulatory functions of some hormones connected with carbohydrate metabolism. and the citric acid cycle.

Xanthine oxidase. cytochrome reductase • FAD: D-amino acid oxidase.• Coenzyme function Examples of flavoprotein enzymes containing FMN and FAD as prosthetic groups are • FMN: Warburg yellow enzyme. the semiquinone form of the isoalloxazine ring is produced. Glycine oxidase. accepting either one or two electrons in the form of one or two hydrogen atoms (each atom an electron plus a proton) from a reduced substrate The fully reduced forms are abbreviated FADH2 and FMNH2. inflammation of the tongue. Vitamin B3 Vitamin B5 Vitamin B6 Folic acid . L-aminoacid oxidase. Thiophorase oxidase. mouth. abbreviated FADH• and FMNH• (stable free radical forms). but the important deficeincy symptoms are cheilosis (Lesions at the mucocutaneous junction at the angles of mouth leading to painful fissures). dermatitis. Active form of vitamin B2 in electron transfers • • • • The succinate formed from succinyl-CoA is oxidized to fumarate by the flavoprotein succinate dehydrogenase in citric acid cycle • • • • • • Deficiency Does not give rise to any clear cut disease. When a fully oxidized flavin nucleotide accepts only one electron (one hydrogen atom). succinate dehydrogenase • The fused ring structure of flavin nucleotides undergoes reversible reduction. fissures in lips. Acyl CoA dehydrogenase.

the equivalent of a proton and two electrons) and is transformed into the reduced form (NADH or NADPH). rice polishing. depending on the isocitrate dehydrogenase isozyme. leafy green vegetables The amino acid tryptophan present in the dietary proteins is converted into niacin in the body. • Coenzyme function NADH and NADPH Act with Dehydrogenases as Soluble Electron Carriers Nicotinamide adenine dinucleotide (NAD in its oxidized form) and its close analog nicotinamide adenine dinucleotide phosphate (NADP) are composed of two nucleotides joined through their phosphate groups by a phosphoanhydride bond Because the nicotinamide ring resembles pyridine. rather. (citric acid cycle) . the “H” denotes the added hydride ion. intestinal tract and the nervous system.  Coenzyme function Enzymes requiring NAD+ or NADH coenzymes are Glyceraldehyde 3-PO4 dehydrogenase Lactate dehydrogenase Ketose reductase Malic dehydrogenase Enzymes requiring NAD+ or NADP+ coenzymes are Isocitrate dehydrogenase Glucose-6-PO4 dehydrogenase Aldolase reductase • The plus sign in the abbreviations NAD and NADP does not indicate the net charge on these molecules (they are both negatively charged). In the abbreviations NADH and NADPH. it indicates that the nicotinamide ring is in its oxidized form. eggs. As a substrate molecule undergoes oxidation (dehydrogenation). • Good sources: Meat. • Fair sources: Milk. with a positive charge on the nitrogen atom.  Functions • Essential for the normal functioning of the skin. the oxidized form of the nucleotide (NAD or NADP) accepts a hydride ion (:H. these compounds are sometimes called pyridine nucleotides. To refer to these nucleotides • • •  Isocitrate binds to the enzyme and is oxidized by hydride transfer to NAD+ or NADP+. tomatoes. giving up two hydrogen atoms. The second proton removed from the substrate is released to the aqueous solvent. liver and poultry.Biotin Vitamin B12 VITAMIN B3 (Nicotinic acid or Niacin)  sources • Best: Yeast. • Used therapeutically for lowering plasma cholesterol.

meat. rice polishings and wheat germ. depression.  AH2 is the reduced substrate and A the oxidized substrate. anxiety. respectively. Pantothenic acid (vit. Rich sources: Yeast. The clinical feature of the disease include-3 D’s Dermatitis --Lesion of skin of face. • NADH and NAD are the reduced and oxidized forms. Good sources: Milk.  • • • • • • • • • • • Deficiency The deficiency of niacin causes the disease pellagra. thick and scaly skin. eggs and leafy vegetables Fair sources: Fruits and other vegetables . knees. In the absence of oxygen pyruvate enters anaerobic phase………. liver. B5) sources Richest source: Jelly. insomnia and forgetfulness. of the coenzyme NAD. breasts. neck. Diarrhoea Dementia—headache.

Coenzyme A combines with acetate to form active acetate (acetyl CoA) combines with oxaloacetic acid to form citric acid-initiates citric acid cycle. . The acyl group such as acetyl or acetoacetyl group is attached to the CoA through a thioester linkage to the Bmercaptoethylamine moiety. The succinyl CoA and glycine are involved in the first step leading to the biosynthesis of heme.• • • • • • • • • Functions Essential for the growth of infants and children. CoA functions in acyl group transfer reactions. acetic acid also combines with cholineàacetyl choline or with sulfonamide drugs which are acetylated prior to excretion CoA in the form of acetyl coA is required for the synthesis of cholesterol and thus steroid hormones. • The decarboxylated product of α –ketoglutarate in citric acid cycle is coenzyme A derivative called active succinate or succinyl CoA. • • • • Coenzyme function In lipid metabolism. Coenzyme function Pantothenic acid is a constituent of Coenzyme A. the fatty acids are to be activated by CoA catalysed by the enzyme thiokinase. Hence anemia occurs in the deficiency of this vitamin. a coenzyme required for the biosynthesis of fatty acids. Significant amount of cellular pantothenic acid is protein bound known as acyl carrier protein. In the form of active acetate. This acetyl CoA directly enters citric acid cycle for the degradation to carbon dioxide and water Or two molecules of acetyl CoA condense to form ketone bodies. In each turn of β oxidation cycle one molecule of acetyl CoA is released. in the first step of oxidation of fatty acids.

• Coenzyme Functions • Essential for the growth of infants. irritability. • PLP functions as codecarboxylase in the decarboxylation of tyrosin. • If ascorbic acid is added to a solution of vitamin B12 . rice polishings. No Toxic effects • Pyridoxine (Vit. B6) • sources • Rich source: Yeast. leafy vegetables and liver. since it provides the complete oxidation of acetyl CoA to carbon dioxide and water. .Note: Citric acid is the common pathway for the metabolism of carbohydrates. • The active coenzyme is pyridoxal 5′-phosphate. • Involved in desulphuration of cysteine and homocysteine. glutamic acid and certain other aminoacids. familial xanthurenic aciduria and some pyridoxal responsive anemias. • Required for brain metabolism because it is necessary for the formation of serotonin. vomiting. Convulsions due to depletion of brain γ. the B12 activity is slowly destroyed due to the reducing action of ascorbic acid on vitamin B12 . certain seeds such as wheat and corn. fats and proteins. • Relationship with oxalate metabolism. Fruits and other vegetables • Intestinal bacteria also synthesize this vitamin. Hypochromic anemia and peripheral neuropathy. • Deficiency Deficiency in man results in nausea. • Good sources: Milk.aminobutyric acid content Inborn errors of metabolism including cystathioninuria. certain gastrointestinal disorders. anemia. fatty liver. meat. arginine. • Fair sources: Fish. • Deficiency Irritability and depression. Toxicity:causes sensory polyneuropathy. • Required for the synthesis of α-aminolevulinic acid which is imp. • PLP catalyses deaminases (dehydrases) for serine and threonine • As a coenzyme for kynureninase in the synthesis of niacin from tryptophan • PLP acts as cotransaminase in the transamination reactions • PLP is required by muscle phosphorylase • PLP acts as coenzyme in transulfuration reaction in the transfer of sulphur from methionine to serine to form cysteine. • Involved in the synthesis of CoA from pantothenic acid • Concerned with immune response. Hyperoxaluria occurs in deficiency states. inadequate growth. failure in gain weights. Folic acid • Tetrahydrofolate • Aqueous solution of vitamin B12 when exposed to sunlight results in the destruction of the vitamin. γ-aminobutyric acid and the catecholamines. intermediate in porphyrin and heme nuclei.

• • Crystalline vitamin B12 is stable to heating at 1000 C for long periods and aqueous solutions at pH 4-7 can be autoclaved with very little loss. Kidney • Good sources: Meat. Hydroxy methyl group: -CH2OH 3. Destruction is rapid when the vitamin is heated at pH 9 or above. The reactions are given below. Biotin • sources . Liver. green leafy vegetables • Fair sources:Milk. choline donate -CH3 group via betain) 4. Formimino group: -CH=NH (Histidine) • Coenzyme Functions Utilisation of one cabon moiety: The single (formyl) carbon present on the tetrahyrofolic acids is utilised in the following ways. methionine. The nuclei of the neutrophil polymorphonuclear leukocytes contain more than the normal number of lobes. i. Conversion of ribonucleotides to deoxyribonucleotides. • Before functioning as C-1 carrier. 5. Conversion of glycine to serine 3.8-dihydrofolic acid (H2 folate) and then to tetrahydro compound (H4 folate) catalysed by folic acid reductase which use NADPH as hydrogen donor. Toxicity: Renal injury. 6. 1. In the formation of N-formyl methionine. C-3 and C-8 positions come through one carbon moiety. Fruits • Intestinal bacteria also synthesize this vitamin.. Other deficiency factors include: retardation of growth. infertility. 7. thymine. inadequate lactation in females and increased output of formiminoglutamic acid (FIGLU) in the urine after histidine loading. folic acid is first reduced to 7. Conversion of uracil to thymine. Since the folic acid coenzymes take part in the synthesis of purines and thymine (methylated pyrimidine of DNA). • sources • Rich source: Yeast. In purine synthesis.e. they are fundamentally involved in the growth and reproduction of cells. • Coenzyme Functions Tetrahydrofolate is the coenzyme form • Folic acid coenzymes are involved in the transfer and utilisation of single or one carbon moiety. Conversion of norepinephrine to epinephrine 4. Fish. • Deficiency Megaloblastic anemia. Methyl group: -CH3 (Homocysteine. Formyl group or formate group: -CHO (α C of glycine and β C of serine are the source of one C moieties) and –HCOOH 2. • One carbon moieties are: 1. Biotin. Conversion of ethanolamine to choline 2.t RNA. weakness.

Absorption depends on the presence of HCl and a constituent of normal gastric juice called the intrinsic factor (IF). Pyruvic acid to Oxaloacetic acid (Gluconeogenesis) is also a biotin dependent carboxylation reaction catalysed by pyruvate carboxylase. and R = CH3 in methylcobalamin. Intestinal bacteria also synthesize this vitamin. a mucopolysaccharide . • Reactions where biotin are involved includes 1. Below the corrin ring is 5. the B12 activity is slowly destroyed due to the reducing action of ascorbic acid on vitamin B12 . Rich source: Egg Yolk. dermatitis. anemia. human milk. R may be varied to give the various forms of the vitamin. tomatoes Fair sources: Fruits.Widely distributed in natural foods. vegetables. muscular pain.6-dimethylbenzimidazole riboside –connected at one end in the central cobalt atom by a nitrogen atom of the nucleotide and at the other end from the ribose moiety through phosphate and aminopropanol to a side chain on ring IV of the tetrapyrrole nucleus. Liver. 2. Cobalt is coordinated to the four nitrogen of the pyrrole rings. Biotin is involved in the fixation of CO2 for the formation of carbon 6 in purine synthesis. Kidney. R = OH– in hydroxocobalamin. Coenzyme function Coenzyme is Biotin carboxyl carrier protein (Biocytin) • Required for carboxylation reactions (CO2 fixation reactions). • Destruction is rapid when the vitamin is heated at pH 9 or above. • If ascorbic acid is added to a solution of vitamin B12 . Two of the pyrrole rings (I and IV) are joined directly. anorexia. • Vitamin B12-cobalamin • Chemistry • Aqueous solution of vitamin B12 when exposed to sunlight results in the destruction of the vitamin. Milk. eg. Absorption and Storage Absorbed from ileum. • Crystalline vitamin B12 is stable to heating at 1000 C for long periods and aqueous solutions at pH 4-7 can be autoclaved with very little loss. R = 5′-deoxyadenosyl in 5′deoxyadenosylcobalamin. Good sources: Yeast. • • • • • • • • • • • • • • Central portion contains reduced and substituted pyrrole rings surrounding a single cobalt atom-referred as corrin ring structure. CO2+NH3 which gives rise to carbamyl phosphate (Urea cycle) 4. Convertion of acetyl CoA to Malonyl CoA (Fatty acid synthesis) in presence of acetyl CoA carboxylase.R = CN– in cyanocobalamin. 3. R = H2O in aquocobalamin. The deficiency develops nausea. • Deficiency Raw egg white induces biotin deficiency because it contains a protein avidin which tightly binds biotin and prevents its absorption from the intestine.

. • Cobalamin bound to plasma protein fraction is carried to the tissues where it is bound to a variety of protein receptors. milk. meat. • Deficiency Pernicious anemia. • Prevention • Vitamin deficiencies can be avoided by the consumption of varieties of food in large quantities to be relieved of the various undesired complications and ailments. Any excess is stored in liver as 51deoxyadenosylcobalamin. • Involved in the biosynthesis of proteins. cheese. Pernicious anemia may also result because of deficiency of intrinsic factor. Also synthesised by intestinal bacteria. Kidney. • Cobalamin unbound to protein is excreted in the urine.(coenzyme for the enzyme mutase) In deficiency methyl malonate accumulates in the urine. egg yolk. fish. Increased excretion of methyl malonic acid in urine No ill effects on excessive ingestion. coenzyme function • Coenzyme in the form of cobamide • Involved in the conversion of L-methyl malonyl coA to succinyl CoA. • Water soluble vitamins must be provided regularly along with food since their storage is limited. • Conversion of glutamic acid to β -methyl aspartic acid • Conversion of ribonucleotides to deoxyribonucleotides • Helps in the synthesis of methyl groups (along with tetrahydrofolate) which can be transferred to homocysteine to form methionine. Sources: Liver. Mucosal atrophy and inflammation of tongue (glottis) and mouth. • Unabsorbed vitamin leaves the body in feces. Severe disease of nervous system-both central and peripheral. • Involved in the maintainance of sulfhydryl groups in the reduced state.secreted by the parietal cells of gastric mucosa which becomes resistant to intestinal digestion. It is not present in foods of plant origin.