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Match the vitamins with their deficiency diseases:
A. Vitamin A → I. Scurvy
B. Vitamin B₁₂ → II. Night blindness
C. Vitamin C → III. Pernicious anaemia
D. Vitamin D → IV. Rickets
Choose the correct match:
Options
1
A-II, B-III, C-I, D-IV
2
A-IV, B-III, C-I, D-II
3
A-III, B-II, C-IV, D-I
4
A-I, B-II, C-III, D-IV
Correct Answer
A-II, B-III, C-I, D-IV
Solution
1

A. Vitamin A → Night blindness (deficiency of retinol impairs rod cell function)

B. Vitamin B₁₂ → Pernicious anaemia (impaired RBC formation)

2

C. Vitamin C → Scurvy (impaired collagen synthesis)

D. Vitamin D → Rickets (impaired calcium absorption and bone mineralisation)

Answer: A-II, B-III, C-I, D-IV

A=Night blindness | B₁₂=Pernicious anaemia | C=Scurvy | D=Rickets
Mnemonic: A→Eyes, B12→Blood, C→Collagen/Scurvy, D→D-bones(Rickets)
Theory: Biomolecules
1. Fat-Soluble Vitamins (A, D, E, K)

Vitamin A (retinol, retinal, retinoic acid): essential for vision (retinal is chromophore in rhodopsin), epithelial cell differentiation, immune function. Deficiency: night blindness, xerophthalmia, keratomalacia. Sources: liver, egg yolk, dairy, carotenoids (carrots, sweet potato). Excess: hypervitaminosis A (liver damage, teratogenic). Vitamin D (cholecalciferol D3, ergocalciferol D2): synthesised in skin from 7-dehydrocholesterol by UV-B. Activated in liver (25-OH) then kidney (1,25-(OH)2 = calcitriol). Promotes intestinal Ca2+ and PO43- absorption. Deficiency: rickets (children — soft bones, bow legs), osteomalacia (adults — bone pain). Excess: hypercalcaemia. Vitamin E (tocopherol): fat-soluble antioxidant. Deficiency: haemolytic anaemia in newborns, ataxia. Vitamin K (phylloquinone K1, menaquinone K2): required for blood clotting factors II, VII, IX, X (carboxylation of glutamate residues). Deficiency: excessive bleeding, haemorrhagic disease of newborn.

2. Water-Soluble Vitamins — B Complex

Vitamin B1 (thiamine): coenzyme in pyruvate dehydrogenase and α-ketoglutarate dehydrogenase. Deficiency: Beriberi (peripheral neuropathy, heart failure) — wet beriberi (oedema) and dry beriberi (neurological). Vitamin B2 (riboflavin): FMN and FAD (electron carriers in respiratory chain). Deficiency: cheilosis, angular stomatitis, glossitis. Vitamin B3 (niacin, nicotinamide): NAD+ and NADP+ (coenzymes in many redox reactions). Deficiency: Pellagra (3Ds: Dermatitis, Diarrhoea, Dementia). Vitamin B5 (pantothenic acid): component of CoA. Deficiency: rare, "burning feet" syndrome. Vitamin B6 (pyridoxine): coenzyme for aminotransferases, decarboxylases. Deficiency: peripheral neuropathy, seborrheic dermatitis, microcytic anaemia. Vitamin B7 (biotin): carboxylation reactions. Deficiency: dermatitis, alopecia (rare — avidin in raw eggs binds biotin). Vitamin B9 (folic acid): one-carbon transfers, essential for DNA synthesis and neural tube development. Deficiency: megaloblastic anaemia, neural tube defects (spina bifida). Vitamin B12 (cobalamin): contains cobalt. Coenzyme for methylmalonyl-CoA mutase and methionine synthase. Deficiency: pernicious anaemia, subacute combined degeneration of spinal cord.

3. Vitamin C (Ascorbic Acid)

Vitamin C is water-soluble, most thermolabile vitamin (destroyed by heat and oxidation). Chemical structure: enediol of lactone of L-gulonic acid. Functions: (1) Coenzyme for hydroxylation of proline and lysine in collagen synthesis (collagen is most abundant protein — 30% of total protein). (2) Antioxidant: reduces oxidative damage. (3) Enhances iron absorption (reduces Fe3+ to Fe2+, which is better absorbed). (4) Immune function: promotes WBC activity. Deficiency — Scurvy: (historically devastated sailors before citrus was discovered). Symptoms: bleeding gums (impaired collagen in blood vessel walls), loose teeth, poor wound healing, perifollicular haemorrhages, corkscrew hairs, anaemia. Source: fresh fruits and vegetables (citrus, kiwi, capsicum, broccoli). RDA: 65-90 mg/day. Linus Pauling controversially advocated megadoses (1-10g/day) for preventing colds — not proven by clinical trials.

4. Vitamin D Metabolism

Vitamin D3 (cholecalciferol) synthesised in skin: 7-dehydrocholesterol + UV-B (290-315 nm) → pre-vitamin D3 → vitamin D3 (thermal isomerisation). Absorbed from diet (D2 or D3 in fortified foods, fatty fish, egg yolk). Liver: 25-hydroxylase → 25-OH-D3 (calcidiol, storage form, measured in blood to assess Vit D status). Kidney: 1α-hydroxylase → 1,25-(OH)2-D3 (calcitriol, active form). Calcitriol binds VDR (Vitamin D Receptor) → nuclear receptor → transcription factor → upregulates calcium transport proteins in intestine, kidney, bone. Rickets prevention: fortified milk, cod liver oil. Vitamin D deficiency is now recognised as epidemic in many countries (indoor lifestyle, sunscreen use, dark skin). Associated with: osteoporosis, increased cancer risk, autoimmune diseases, cardiovascular disease. Daily sunlight exposure (15-20 min, arms and legs) generates 10,000-25,000 IU vitamin D3.

5. Proteins — Structure and Function

Proteins: polymers of amino acids linked by peptide bonds (-CO-NH-). 20 standard amino acids. Primary structure: sequence of amino acids. Secondary structure: α-helix (right-handed, 3.6 residues/turn, H-bonds within chain), β-pleated sheet (H-bonds between chains), β-turns. Tertiary structure: 3D fold stabilised by: disulphide bonds (Cys-Cys), hydrophobic interactions, ionic bonds (salt bridges), H-bonds. Quaternary structure: association of multiple subunits. Haemoglobin: 4 subunits (2α+2β), cooperative O2 binding. Denaturation: loss of 3D structure by heat, acid, base, heavy metals, detergents. Primary structure maintained (peptide bonds intact). Biological activity lost. Sometimes reversible (renaturation). Enzymes: biological catalysts, protein in nature (except ribozymes). Active site is critical for function. Allosteric enzymes: regulated by molecules binding at sites other than active site.

6. Carbohydrates

Monosaccharides: simplest carbohydrates. Aldoses (CHO group) and ketoses (C=O group). D-glucose (aldohexose): most important fuel. D-fructose (ketohexose): fruits. Galactose: in lactose. Ribose, deoxyribose: in nucleic acids. Disaccharides: maltose (glucose-glucose, α-1,4), sucrose (glucose-fructose, α-1,β-2), lactose (galactose-glucose, β-1,4). Reducing sugars: free aldehyde/ketone group, react with Fehlings, Benedicts, Tollens. Sucrose: non-reducing (glycosidic bond between anomeric carbons of both sugars). Polysaccharides: starch (amylose α-1,4 + amylopectin α-1,4 and α-1,6). Glycogen (α-1,4 and α-1,6, more branched than amylopectin). Cellulose (β-1,4, structural, humans cannot digest). Chitin (β-1,4-N-acetylglucosamine, fungal cell walls, insect exoskeleton).

7. Nucleic Acids

DNA: deoxyribonucleic acid. Double helix (Watson-Crick, 1953). Antiparallel strands. Base pairs: A=T (2 H-bonds), G≡C (3 H-bonds). Sugar: deoxyribose. Backbone: phosphodiester bonds (5→3 direction). B-form DNA: 10 bp/turn, pitch 34 Å. A-form (less common): 11 bp/turn. Z-form (left-handed): in GC-rich sequences. RNA: ribonucleic acid. Single-stranded (mostly). Sugar: ribose (2-OH group present). Uracil replaces thymine. Types: mRNA (messenger), tRNA (transfer, cloverleaf secondary structure, anticodon loop, CCA-3 for amino acid attachment), rRNA (ribosomal, structural). Nucleotides: base + sugar + phosphate. Nucleosides: base + sugar. ATP: adenosine triphosphate, universal energy currency. High-energy phosphoanhydride bonds. ΔG° for hydrolysis = -30.5 kJ/mol.

8. Lipids

Lipids: diverse group of biological molecules soluble in organic solvents (hydrophobic). Fats and oils: triacylglycerols (triglycerides). Fatty acids + glycerol. Saturated (no double bonds): palmitic (C16), stearic (C18). Solid at room temperature. Animal fats. Unsaturated (one or more C=C): oleic (C18:1, cis), linoleic (C18:2, ω-6), linolenic (C18:3, ω-3). Liquid at room temperature. Plant/fish oils. Saponification: triglyceride + NaOH → soap (sodium salt of fatty acid) + glycerol. Soap: hydrophilic head (-COO-Na+) and hydrophobic tail (long carbon chain). Micelles in water. Phospholipids: membrane components. Glycerophospholipids: glycerol backbone. Lecithin (phosphatidylcholine): major membrane component, emulsifier. Steroids: four-ring structure. Cholesterol: membrane component, precursor to hormones. Bile salts, sex hormones (testosterone, oestrogen), adrenocortical hormones (cortisol, aldosterone), vitamin D. Waxes: long chain fatty acid esterified with long chain alcohol. Beeswax (myricyl palmitate). Protective function.

Frequently Asked Questions
1. How does Vitamin A function in vision?
Vitamin A (all-trans retinol) is converted to 11-cis retinal in the retina. 11-cis retinal combines with the protein opsin to form rhodopsin (rod cell pigment). When light hits rhodopsin: 11-cis retinal → all-trans retinal (photoisomerisation). This conformational change triggers a nerve impulse (phototransduction cascade involving G-protein transducin, PDE, cGMP, ion channels). All-trans retinal is released from opsin → re-isomerised to 11-cis retinal (requires vitamin A). In vitamin A deficiency: rhodopsin cannot be regenerated → impaired vision in dim light (night blindness). Severe deficiency: xerophthalmia (dry eye) → corneal ulceration → blindness.
2. What is pernicious anaemia and how is it different from other anaemias?
Pernicious anaemia: megaloblastic anaemia caused by inability to absorb vitamin B12. Not due to dietary deficiency (B12 is stored for years in liver). Cause: lack of intrinsic factor (IF) — a glycoprotein made by gastric parietal cells. IF binds B12 in stomach → B12-IF complex absorbed in terminal ileum. Without IF: B12 not absorbed → deficiency. Gastric parietal cell destruction (autoimmune atrophic gastritis) causes pernicious anaemia. Treatment: monthly B12 injections (bypass intestinal absorption). B12 is needed for: (1) Methionine synthase (methionine from homocysteine + methyltetrahydrofolate). (2) Methylmalonyl-CoA mutase (converts methylmalonyl-CoA to succinyl-CoA — important in myelin synthesis). Deficiency also causes subacute combined degeneration of spinal cord (demyelination).
3. Why does Vitamin C deficiency cause scurvy?
Vitamin C (ascorbic acid) is an essential cofactor for: (1) Prolyl hydroxylase and lysyl hydroxylase — enzymes that hydroxylate proline and lysine residues in procollagen. These hydroxyproline and hydroxylysine residues are critical for: triple helix formation in collagen (hydroxyproline provides H-bonds that stabilise the triple helix). Cross-linking between collagen fibrils (hydroxylysine provides sites for galactosylation and cross-link formation). Without vitamin C: defective collagen synthesised → weak connective tissue → bleeding from blood vessels (perivascular haemorrhage), loose teeth (periodontal ligament fails), poor wound healing, bone abnormalities. Historical importance: scurvy killed more sailors than battles until Lind discovered citrus fruits prevented it (1747). James Cook's voyages (1770s) used lemon/lime juice routinely.
4. What are the differences between fat-soluble and water-soluble vitamins?
Fat-soluble (A, D, E, K): absorbed with dietary fat in lymphatics, stored in liver and adipose tissue for months to years. Not excreted in urine. Excess causes toxicity (hypervitaminosis A: headache, liver damage, teratogenic; D: hypercalcaemia, calcium deposits). Deficiency develops slowly. Can be taken weekly or monthly. Water-soluble (B-complex, C): absorbed directly into blood. Not stored significantly (except B12 — 3-5 year supply in liver). Excreted in urine when excess. Toxicity rare (except B6 at megadoses → peripheral neuropathy). Deficiency develops quickly. Need regular daily intake. Practical implications: fat malabsorption (coeliac, Crohn, cholestasis) → deficiency of fat-soluble vitamins. Total parenteral nutrition patients need careful monitoring of fat-soluble vitamins. Vegan diet: risk of B12 deficiency (B12 only in animal products). Elderly with achlorhydria: B12 deficiency risk.
5. What is the role of Vitamin K in blood clotting?
Vitamin K is essential for the post-translational modification (carboxylation) of glutamate residues to gamma-carboxyglutamate (Gla) in clotting factors II (prothrombin), VII, IX, X, and proteins C and S. These Gla residues bind Ca2+ ions, which allow the clotting factors to bind to phospholipid membranes of platelets and endothelium — an essential step in the coagulation cascade. Without vitamin K: clotting factors are inactive → coagulopathy → excessive bleeding. Warfarin (and other coumarin anticoagulants) work by inhibiting vitamin K epoxide reductase — the enzyme that regenerates active vitamin K from its epoxide form after carboxylation reactions. Neonates have low vitamin K (minimal placental transfer, sterile gut with no K2-producing bacteria) → given vitamin K injection at birth to prevent haemorrhagic disease of the newborn.
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