Zoology 2024 Paper II 50 marks Describe

Paper II — Q7

(a) Describe the process of spermatogenesis. Add a note on the role of Golgi bodies in the formation of acrosome. (15+5=20…

(a)

Describe the process of spermatogenesis. Add a note on the role of Golgi bodies in the formation of acrosome. (15+5=20 marks)

(b)

Why are vitamins also called coenzymes? Justify. 15 marks

(c)

Explain the mechanism of contraction in skeletal muscle. What do you mean by Rheobase and Chronaxie? (12+3=15 marks)

हिंदी में प्रश्न पढ़ें
(a)

शुक्राणुजनन की प्रक्रिया का वर्णन कीजिए। अग्रपिंडक के निर्माण में गॉल्जी काय की भूमिका पर एक टिप्पणी लिखिए। (15+5=20 अंक)

(b)

विटामिनों को सह-एंजाइम भी क्यों कहा जाता है? सिद्ध कीजिए। (15 अंक)

(c)

कंकाल पेशी में संकुचन की क्रियाविधि की व्याख्या कीजिए। अलिबंधारा (रियोबेस) व कालमान (क्रोनेक्सी) से आप क्या समझते हैं? (12+3=15 अंक)

Q7 of the 2024 UPSC Mains Zoology Paper II, as printed
The question as printed in the 2024 Zoology paper

Model answer

Drafted with AI by UPSC Answer Check against this question's marking rubric, to the expected length. UPSC does not publish answers for Mains — this is one way to score well, not an official key. How we build rubrics and answers.

(a)(i) Process of Spermatogenesis

Spermatogenesis is the continuous process occurring within the seminiferous tubules of testes, wherein diploid spermatogonia transform into haploid spermatozoa. It proceeds through three major phases: the proliferative phase, meiotic phase, and spermiogenesis.

Type A spermatogonia undergo mitotic divisions to maintain the stem cell pool and yield Type B spermatogonia, which enlarge into primary spermatocytes (46, XY). Under the influence of follicle-stimulating hormone (FSH) acting on Sertoli cells and luteinizing hormone (LH) stimulating Leydig cells to secrete testosterone, primary spermatocytes undergo Meiosis I to form two haploid secondary spermatocytes (23, X or 23, Y). These rapidly enter Meiosis II, producing four non-motile, spherical spermatids.

During spermiogenesis, spermatids differentiate into spermatozoa without further division: the nucleus condenses as histones are replaced by protamines, the distal centriole forms the axoneme of the flagellum, mitochondria wrap spirally round the middle piece, and excess cytoplasm is shed as residual bodies that Sertoli cells phagocytose. Sertoli cells also form the blood–testis barrier and nourish the germ cells, and mature sperm are released into the lumen by spermiation. In humans one cycle from spermatogonium to sperm takes about 64–74 days.

Diagram: Seminiferous tubule

(a)(ii) Role of Golgi Bodies in Acrosome Formation

The Golgi apparatus plays a central role in generating the acrosome, an apical cap acting as a specialized lysosome. Acrosome formation passes through the Golgi, cap, acrosome and maturation phases. Ultrastructurally, the Golgi cisternae produce multiple electron-dense proacrosomal vesicles that coalesce into a single large acrosomal vesicle containing an acrosomal granule. This vesicle adheres to the nuclear membrane at the anterior pole of the condensing nucleus, spreading over its anterior two-thirds to form the acrosomal cap. The remnant Golgi apparatus moves away as the Golgi remnant. The completed acrosome contains hydrolytic enzymes, notably hyaluronidase, corona penetrating enzyme, and acrosin, which are essential for penetrating the cumulus oophorus and zona pellucida during fertilization.

Diagram: Acrosome formation

(b) Why Vitamins Are Called Coenzymes

Vitamins, specifically water-soluble B-complex vitamins, are designated as coenzymes because they serve as essential, non-protein organic precursors that bind with apoenzymes to form catalytically active holoenzymes. Unlike macronutrients, vitamins function catalytically in micro-quantities rather than stoichiometrically as substrates.

The biochemical justification rests on their obligate transformation into reactive prosthetic groups or co-substrates: Thiamine (Vitamin B1) is phosphorylated to Thiamine Pyrophosphate (TPP) for oxidative decarboxylation; Riboflavin (Vitamin B2) forms Flavin Mononucleotide (FMN) and Flavin Adenine Dinucleotide (FAD) for cellular redox reactions; Niacin (Vitamin B3) yields NAD+ and NADP+, serving as universal hydride-ion carriers; Pantothenic acid (Vitamin B5) forms the functional core of Coenzyme A for acyl transfers; Pyridoxine (Vitamin B6) converts to Pyridoxal Phosphate (PLP) for transamination and amino acid metabolism; Biotin (Vitamin B7) acts as a covalently bound coenzyme in carboxylation reactions; Folic acid (Vitamin B9) converts to Tetrahydrofolate (THF) for one-carbon unit transfer; and Cobalamin (Vitamin B12) forms Methylcobalamin and Adenosylcobalamin for isomerase and methyltransferase reactions. Strictly, the vitamin is the precursor and its derivative is the coenzyme, which is why deficiency of a vitamin shows up as failure of particular enzymes: TPP deficiency causes beriberi, NAD deficiency pellagra, and folate or B12 deficiency megaloblastic anaemia.

Unlike fat-soluble vitamins (A, D, E, K), which primarily function as nuclear receptor ligands, visual pigments or lipid-soluble antioxidants (although vitamin K is a true cofactor for γ-glutamyl carboxylase in clotting-factor synthesis, and vitamin C for prolyl and lysyl hydroxylases in collagen synthesis), water-soluble vitamins undergo limited tissue storage and function directly in intermediary metabolic enzymatic complexes.

(c)(i) Mechanism of Contraction in Skeletal Muscle

Skeletal muscle contraction operates via the sliding filament mechanism coupled with excitation-contraction coupling. At the neuromuscular junction, acetylcholine released from the motor nerve ending binds nicotinic receptors and produces an end-plate potential that triggers a muscle action potential, which propagates across the sarcolemma and down the transverse (T) tubules. This depolarizes dihydropyridine receptors, opening ryanodine receptors on the sarcoplasmic reticulum to release Ca²⁺ into the sarcoplasm.

Elevated Ca²⁺ binds to troponin C, producing a conformational shift in troponin I and troponin T that pulls tropomyosin away from actin active sites. Myosin heads, energized by hydrolyzed ATP (bound to ADP and Pi), bind to exposed actin to form cross-bridges. The release of Pi and ADP triggers the power stroke, tilting the myosin head by 45 degrees and pulling the thin actin filament toward the center of the sarcomere (H-zone narrowing). Binding of a new ATP molecule causes myosin detachment; ATP hydrolysis re-cocks the head for subsequent cycling until Ca²⁺ is actively pumped back by SERCA pumps. During contraction the A band keeps its length while the I band and H zone shorten, because the filaments slide rather than shorten; without ATP the cross-bridges cannot detach, which explains rigor mortis.

Diagram: Muscle contraction

(c)(ii) Rheobase and Chronaxie

Neuromuscular excitability is evaluated using the strength-duration curve. Rheobase is defined as the minimum galvanic electrical stimulus intensity (current or voltage) of infinite duration required to elicit a threshold muscle contraction. Chronaxie is the minimum stimulus duration required to excite the tissue when using a current twice the strength of the rheobase. Chronaxie provides a precise index of excitability: tissues with shorter chronaxie values, such as myelinated nerves and fast skeletal muscle fibers, exhibit higher excitability.

Diagram: Strength-duration curve

How this answer will be evaluated

Framework: Zoology Paper 2: Define > Structure/Mechanism > Diagram > Example

What earns full marks: Precise terminology, labelled diagrams, and clear logical flow for all parts.

Evaluation rubric

Each sub-part is marked on its own, against the marks and word limit printed on the paper.

  1. (a)(i) (a)(i) Process of spermatogenesis (15 marks) 15 marks

    Must cover

    • Site: seminiferous tubules; roles of Sertoli (support, blood–testis barrier) and Leydig cells (testosterone)
    • Phases: multiplication (spermatogonia A and B), growth (primary spermatocyte), maturation (meiosis I and II) with chromosome numbers
    • Spermiogenesis: nuclear condensation, acrosome, flagellum from distal centriole, mitochondrial sheath, loss of cytoplasm; spermiation
    • Hormonal control by FSH, LH/testosterone and inhibin; duration ~64–74 days

    Loses marks

    • Wrong ploidy at stages
    • Confusing spermatogenesis with spermiogenesis

    Earns more

    • Labelled diagram of tubule section and sperm
    • Comparison with oogenesis

    Extra mark

    • Clonal syncytia via cytoplasmic bridges
  2. (a)(ii) (a)(ii) Role of Golgi bodies in acrosome formation (5 marks) 5 marks

    Must cover

    • Golgi produces proacrosomal granules/vesicles
    • Fusion into single acrosomal vesicle with granule attaching to the nucleus
    • Spreading as acrosomal cap; Golgi remnant discarded
    • Phases (Golgi, cap, acrosome, maturation) and enzymes (hyaluronidase, acrosin) for fertilisation

    Loses marks

    • Deriving acrosome from mitochondria
    • No enzyme content

    Earns more

    • Stage diagrams
    • Acrosome as a modified lysosome

    Extra mark

    • Acrosome reaction at fertilisation
  3. (b) (b) Why are vitamins called coenzymes? Justify (15 marks) 15 marks

    justify— claim → 3-4 reasons → evidence → conclusion

    Must cover

    • Concept of apoenzyme + coenzyme = holoenzyme; vitamins as precursors of coenzymes needed in catalytic amounts
    • B-complex examples: B1→TPP, B2→FMN/FAD, B3→NAD/NADP, B5→CoA, B6→PLP, B7→biotin, B9→THF, B12→cobamides with reactions
    • Fat-soluble vitamins mostly not coenzymes (except K as carboxylase cofactor); vitamin C as hydroxylase cofactor
    • Deficiency diseases showing enzyme failure (beriberi, pellagra, megaloblastic anaemia)

    Loses marks

    • Claiming all vitamins are coenzymes
    • Wrong vitamin–coenzyme pairing

    Earns more

    • Structural features (e.g. nicotinamide ring)
    • Mechanistic examples (PLP in transamination)

    Extra mark

    • Riboflavin in electron transport chain
  4. (c)(i) (c)(i) Mechanism of contraction in skeletal muscle (12 marks) 12 marks

    Must cover

    • Neuromuscular transmission: ACh, nicotinic receptor, end-plate potential, muscle action potential
    • Excitation–contraction coupling: T-tubules, DHP receptors, ryanodine receptors, Ca²⁺ release
    • Ca²⁺–troponin C, tropomyosin shift, cross-bridge cycle with ATP (attachment, power stroke, detachment)
    • Sliding filament evidence (A band constant, I band and H zone shorten); relaxation by SERCA

    Loses marks

    • Saying filaments shorten
    • Omitting Ca²⁺ role

    Earns more

    • Sarcomere diagram
    • Rigor mortis explanation

    Extra mark

    • Huxley and Hanson sliding filament theory
  5. (c)(ii) (c)(ii) Rheobase and chronaxie (3 marks) 3 marks

    Must cover

    • Strength–duration curve
    • Rheobase: minimum current strength that excites when applied for long duration
    • Chronaxie: minimum duration needed at twice the rheobase
    • Use as an index of excitability (shorter chronaxie = more excitable)

    Loses marks

    • Swapping definitions
    • No reference to twice rheobase

    Earns more

    • Diagram of the curve
    • Clinical use in nerve injury

    Extra mark

    • Utilisation time concept
What "Describe" is asking you to do

Give a full, ordered account of the thing named — its parts, stages or mechanism — in the sequence in which it actually exists or occurs. Most describe questions come from the science optionals, where the marks sit in correct technical detail and, where the stem says so, a labelled diagram.

Structure that answers it

One-line identification of the subject → the parts or stages in their real order, each with its defining detail → labelled diagram where the subject is structural → closing line on function or significance

Where marks are lost

Loose general prose where the examiner is ticking named parts, correct terminology and their sequence; and in the General Studies papers, turning to evaluation before the description is finished.

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