Catecholamines are synthesized from?
Which of the following amino acids is not involved in the production of creatine?
Ninhydrin test is used for?
Which enzyme catalyzes oxidative deamination?
Transamination of Aspartate forms which compound?
Clinical effect of vitamin D is reduced by ?
What is the number of variable regions present on each light and heavy chain of an antibody?
All of the following are required more during lactation as compared to pregnancy, except ?
What is the iron requirement for a normal menstruating adult female?
Which nut has the highest protein content among the following options?
NEET-PG 2013 - Biochemistry NEET-PG Practice Questions and MCQs
Question 111: Catecholamines are synthesized from?
- A. Tyrosine (Correct Answer)
- B. Histidine
- C. Methionine
- D. Tryptophan
Explanation: ***Tyrosine*** - **Tyrosine** is the direct precursor amino acid for the synthesis of all **catecholamines**, including **dopamine**, **norepinephrine**, and **epinephrine**. - The synthesis pathway begins with the conversion of tyrosine to **L-DOPA** by tyrosine hydroxylase, followed by subsequent enzymatic steps. *Methionine* - **Methionine** is an essential amino acid primarily involved in **protein synthesis** and as a precursor for S-adenosylmethionine (SAM), a key methyl donor in various metabolic reactions. - It is not a direct precursor for the synthesis of **catecholamines**. *Histidine* - **Histidine** is the precursor for the synthesis of **histamine**, a neurotransmitter and inflammatory mediator. - It is not involved in the biosynthesis pathway of **catecholamines**. *Tryptophan* - **Tryptophan** is the precursor for the synthesis of **serotonin** and **melatonin**, important neurotransmitters and hormones. - It does not play a role in the synthesis of **catecholamines**.
Question 112: Which of the following amino acids is not involved in the production of creatine?
- A. Glycine
- B. Methionine
- C. Alanine (Correct Answer)
- D. Arginine
Explanation: ***Alanine*** - **Alanine** is not directly involved as a precursor for **creatine synthesis**. It can be converted to pyruvate and enter the gluconeogenic pathway. - The primary amino acids involved in **creatine synthesis** are arginine, glycine, and methionine. *Glycine* - **Glycine** is a direct precursor for creatine, reacting with arginine in the first step of its synthesis to form **guanidinoacetate**. - This reaction is catalyzed by **arginine:glycine amidinotransferase (AGAT)**. *Methionine* - **Methionine**, in the form of **S-adenosylmethionine (SAM)**, acts as the methyl donor in the second step of creatine synthesis. - It methylates guanidinoacetate to form **creatine**, a reaction catalyzed by **guanidinoacetate methyltransferase (GAMT)**. *Arginine* - **Arginine** donates its guanidino group to glycine, forming **guanidinoacetate**, the initial intermediate in creatine synthesis. - This is the first committed step in the **creatine biosynthesis pathway**.
Question 113: Ninhydrin test is used for?
- A. Bile salts
- B. Amino acids (Correct Answer)
- C. Nucleic acid
- D. Lipids
Explanation: ***Amino acids*** - The **ninhydrin test** is a chemical test used to detect the presence of **amino acids** and primary and secondary amines. - It produces a **purple-blue color** when it reacts with most amino acids, due to the formation of a colored complex called Ruhemann's purple. *Bile salts* - The detection of **bile salts** typically involves tests like Hay's test or Pettenkofer's test, which are distinct from the ninhydrin reaction. - These tests rely on the physical or chemical properties of bile salts, such as changes in surface tension or specific color reactions with sulfuric acid. *Nucleic acid* - **Nucleic acids** (DNA and RNA) are detected using specific tests like the **diphenylamine test** (for DNA) or orcinol test (for RNA). - These tests target the deoxyribose or ribose sugars present in their structures and result in different color changes compared to ninhydrin. *Lipids* - **Lipids** are typically identified using tests that exploit their nonpolar nature, such as the **emulsion test** or solubility tests in organic solvents. - Their detection does not involve ninhydrin, as they lack the primary or secondary amine groups that react with this reagent.
Question 114: Which enzyme catalyzes oxidative deamination?
- A. Glutaminase
- B. Glutamine synthase
- C. Glutamate dehydrogenase (Correct Answer)
- D. None of the options
Explanation: ***Glutamate dehydrogenase*** - This enzyme catalyzes the conversion of **glutamate** to **α-ketoglutarate** and ammonia (NH₃), which is an oxidative deamination reaction. - It utilizes **NAD⁺ or NADP⁺** as a coenzyme to remove hydrogen atoms during the oxidation process. - Plays a crucial role in both **amino acid catabolism** and anabolism. *Glutaminase* - This enzyme hydrolyzes **glutamine** to glutamate and ammonia, which is a **hydrolytic deamidation** reaction, not an oxidative deamination. - It does not involve the oxidation of the substrate or require NAD⁺/NADP⁺ as cofactors. *Glutamine synthase* - This enzyme synthesizes **glutamine** from glutamate and ammonia, using ATP, which is a **biosynthetic** reaction, not a catabolic deamination. - It is involved in **ammonia detoxification** and amino acid synthesis, functioning in the opposite direction of deamination. *None of the options* - This option is incorrect because **glutamate dehydrogenase** is a valid correct answer. - Glutamate dehydrogenase is the primary enzyme responsible for oxidative deamination in human metabolism.
Question 115: Transamination of Aspartate forms which compound?
- A. Pyruvate
- B. Acetyl-CoA
- C. Oxaloacetate (Correct Answer)
- D. Alanine
Explanation: ***Oxaloacetate*** - **Aspartate** is transaminated by **aspartate aminotransferase (AST)**, transferring its alpha-amino group to **alpha-ketoglutarate**. - This reaction converts aspartate into its corresponding alpha-keto acid, which is **oxaloacetate**. *Pyruvate* - **Pyruvate** is the alpha-keto acid corresponding to the amino acid **alanine**. - Transamination of **alanine** yields **pyruvate**, not aspartate. *Acetyl-CoA* - **Acetyl-CoA** is not a direct product of amino acid transamination; it is formed from **pyruvate** or fatty acid oxidation. - It functions as a key metabolic intermediate in energy production and biosynthesis. *Alanine* - **Alanine** is an amino acid, and therefore a reactant in transamination reactions to form pyruvate, rather than a product of aspartate transamination. - While it can be formed from pyruvate via transamination, it is not formed from aspartate.
Question 116: Clinical effect of vitamin D is reduced by ?
- A. Simultaneous ingestion of lactose
- B. Simultaneous ingestion of phytates (Correct Answer)
- C. None of the options
- D. Acidic environment
Explanation: ***Simultaneous ingestion of phytates*** - **Phytates (phytic acid)** found in whole grains, nuts, seeds, and legumes can **reduce the clinical effect of vitamin D** through multiple mechanisms - Phytates **chelate calcium** and form insoluble calcium-phytate complexes, reducing calcium absorption - Since **vitamin D and calcium metabolism are closely linked**, impaired calcium absorption indirectly reduces vitamin D efficacy - Phytates can also **directly bind to vitamin D** in the gastrointestinal tract, reducing its bioavailability - Studies show that **high phytate intake increases vitamin D requirements** and can impair vitamin D status *Simultaneous ingestion of lactose* - Lactose does **not reduce** vitamin D absorption or efficacy - In fact, **dairy products are commonly fortified** with vitamin D, and the presence of lactose does not interfere with its beneficial effects - Lactose may actually **enhance calcium absorption**, which works synergistically with vitamin D *Acidic environment* - Vitamin D is a **fat-soluble vitamin** absorbed primarily in the small intestine - An acidic environment (stomach acid) is **not known to inhibit** vitamin D absorption - The absorption process occurs in the **alkaline environment of the small intestine** where fat-soluble vitamins are absorbed with dietary fats *None of the options* - This is **incorrect** as phytates do reduce the clinical effect of vitamin D through calcium chelation and direct binding mechanisms
Question 117: What is the number of variable regions present on each light and heavy chain of an antibody?
- A. 1 (Correct Answer)
- B. 2
- C. 3
- D. 4
Explanation: ***1*** - Each **light chain** and **heavy chain** within an antibody molecule contains **one variable region (V domain)**. - These variable regions are crucial for **antigen binding specificity**, as they combine to form the antigen-binding site. - The variable domain is located at the **N-terminal end** of each chain. *2* - While a complete antibody molecule has **two antigen-binding sites** (bivalent), each formed by pairing of VH and VL domains, individual chains possess only **one variable region each**. - The number '2' refers to the total number of identical binding sites on the intact antibody, not the number of variable regions per chain. *3* - The number **3** does not correspond to the number of variable regions on individual chains. - This might be confused with the **three complementarity-determining regions (CDRs)** present within each variable domain (CDR1, CDR2, CDR3), which are hypervariable loops that directly contact the antigen. *4* - The number **4** is incorrect for variable regions. - This number corresponds to the total number of **polypeptide chains** in a complete IgG antibody (2 heavy + 2 light chains), or the number of **constant domains** in some heavy chain isotypes (IgM, IgE have 4 CH domains).
Question 118: All of the following are required more during lactation as compared to pregnancy, except ?
- A. Niacin
- B. Energy
- C. Iron (Correct Answer)
- D. Vitamin A
Explanation: ***Iron*** - **Iron requirements are significantly higher during pregnancy** (~27 mg/day) due to the expansion of maternal red blood cell mass, fetal development, and placental iron needs. - During lactation, iron requirement decreases to **~9-10 mg/day**, lower than in pregnancy, as **lactational amenorrhea** (absence of menstruation) reduces iron loss. - This represents the **most significant decrease** in requirement from pregnancy to lactation among the listed nutrients. *Vitamin A* - The **recommended daily allowance (RDA) for Vitamin A is higher during lactation** (~1300 μg/day) compared to pregnancy (~800 μg/day). - This increased requirement ensures **adequate transfer to breast milk** to support infant's **vision development and immune function**. *Niacin* - **Niacin requirements during lactation** (~17 mg/day) are **similar to pregnancy** (~18 mg/day). - While lactation involves increased metabolic demands, niacin requirements do not show a marked increase compared to pregnancy, unlike Vitamin A and Energy. - This option is less clearly "required more" during lactation. *Energy* - **Energy requirements are significantly higher during lactation** to fuel milk production, which is energetically demanding. - A lactating woman typically needs an **additional 500 kcal/day**, compared to ~300 kcal/day in the 2nd/3rd trimester of pregnancy.
Question 119: What is the iron requirement for a normal menstruating adult female?
- A. 30 mg/day
- B. 35 mg/day
- C. 20 mg/day
- D. 15 mg/day (Correct Answer)
Explanation: ***15 mg/day*** - The recommended daily iron intake for a normal menstruating adult female was **15 mg/day** according to guidelines at the time of this examination (NEET-2013). - This higher requirement compared to males and post-menopausal women is due to **iron loss in menstrual blood**, averaging approximately **0.5-1 mg/day** additional iron loss. - **Note:** Current guidelines recommend **18 mg/day** (US RDA) or **21 mg/day** (ICMR, India), but this question reflects the 2013 standard. *20 mg/day* - This amount is **higher than the typical recommendation** for healthy menstruating women without significant pathology. - While some women with heavier menstrual bleeding might require this, it's not the baseline requirement for normal menstruation. *30 mg/day* - This intake level is typically recommended for **pregnant women** in the second and third trimesters or individuals with **diagnosed iron deficiency anemia** requiring therapeutic supplementation. - It is significantly more than the daily requirement for a healthy menstruating female. *35 mg/day* - This is an **excessively high** daily iron intake for a healthy menstruating female. - Such high doses are usually prescribed for **severe iron deficiency anemia** or specific medical conditions under supervision. - Chronic intake at this level without medical indication could potentially lead to adverse effects.
Question 120: Which nut has the highest protein content among the following options?
- A. Walnut
- B. Coconut
- C. Groundnut (Correct Answer)
- D. Almond
Explanation: ***Groundnut*** - **Groundnuts** (peanuts) contain approximately **26 grams of protein per 100 grams**, which is the highest among the given options. - While botanically classified as legumes, groundnuts are commonly grouped with nuts in nutritional contexts. - They are also rich in **healthy fats**, **fiber**, and various **B vitamins**. *Almond* - **Almonds** contain about **21 grams of protein per 100 grams**, making them the second highest in protein content among the options. - They are excellent sources of **vitamin E**, **magnesium**, and **healthy monounsaturated fats**. *Walnut* - **Walnuts** contain approximately **15 grams of protein per 100 grams**, which is lower than both groundnuts and almonds. - They are notably rich in **omega-3 fatty acids** (alpha-linolenic acid). *Coconut* - **Coconut flesh** has relatively low protein content, around **3.3 grams per 100 grams**. - It is primarily known for its high content of **medium-chain triglycerides** and **saturated fats**.