What is the classification of Carcinoembryonic Antigen (CEA)?
Level of which of the following is not elevated in heart disease
The predominant isozyme of LDH in lung is:
What is the primary receptor for High-Density Lipoprotein (HDL) in cholesterol metabolism?
What is the primary role of calnexin and calreticulin in the endoplasmic reticulum?
Which gene is responsible for the production of COX type 3?
Which of the following statements are true regarding the visual cycle cascade?
Which of the following proteins is primarily responsible for marking other proteins for degradation?
GlcNAc-P-P-oligosaccharide is -
Prolyl hydroxylase requires which cofactor?
NEET-PG 2015 - Biochemistry NEET-PG Practice Questions and MCQs
Question 81: What is the classification of Carcinoembryonic Antigen (CEA)?
- A. Glycoprotein (Correct Answer)
- B. Lipoprotein
- C. Phosphoprotein
- D. Nucleoprotein
Explanation: ***Glycoprotein*** - Carcinoembryonic Antigen (CEA) is classified as a **glycoprotein** due to its structure, which consists of both **carbohydrate** and **protein** components. - This glycosylation is crucial for its function as a cell adhesion molecule and its recognition in diagnostic assays. *Lipoprotein* - **Lipoproteins** are complexes of lipids and proteins that function primarily in **lipid transport** in the blood. - CEA's primary role and structure are not related to lipid transport or being predominantly lipid-based. *Phosphoprotein* - A **phosphoprotein** is a protein that has been **covalently modified by the addition of a phosphate group**, a process crucial for cell signaling. - While proteins can be phosphorylated, the defining characteristic and major classification of CEA is its extensive glycosylation rather than phosphorylation state. *Nucleoprotein* - **Nucleoproteins** are proteins that are **structurally associated with nucleic acids** (DNA or RNA), such as histones or ribosomal proteins. - CEA does not have a structural or functional association with nucleic acids.
Question 82: Level of which of the following is not elevated in heart disease
- A. SGOT
- B. ALP
- C. LDH
- D. 5-nucleotidase (Correct Answer)
Explanation: ***5-nucleotidase*** - While other enzymes like LDH, SGOT, and ALP can be elevated in various conditions including heart disease (especially in the context of tissue damage), 5-nucleotidase is **not typically elevated in heart disease**. - Its elevation is more commonly associated with **biliary obstruction** or certain liver pathologies. *LDH* - **Lactate dehydrogenase (LDH)** is a marker of **cellular damage** and can be elevated in myocardial infarction, though it is less specific than troponins. - LDH levels rise later than CK-MB and remain elevated longer, indicating persistent tissue injury. *SGOT* - **Serum glutamic oxaloacetic transaminase (SGOT)**, also known as **aspartate aminotransferase (AST)**, is elevated in acute **myocardial infarction** due to cardiac muscle damage. - While it's a marker for cardiac injury, it's not specific as it's also highly concentrated in the liver. *ALP* - **Alkaline phosphatase (ALP)** can be mildly elevated in heart failure due to **hepatic congestion** caused by reduced cardiac output. - While its primary diagnostic significance is in bone and liver disease, its elevation in advanced heart disease is usually a secondary consequence.
Question 83: The predominant isozyme of LDH in lung is:
- A. LD-2
- B. LD-5
- C. LD-1
- D. LD-3 (Correct Answer)
Explanation: ***LD-3*** - **LD-3** is the predominant **LDH isozyme** found in the **lungs**, spleen, pancreas, and lymph nodes. - Its elevation often suggests conditions affecting these organs, such as pulmonary embolism or pancreatitis. *LD-1* - **LD-1** is primarily associated with the **heart** and **red blood cells**. - Elevated levels are typically seen in conditions like myocardial infarction and hemolytic anemia. *LD-2* - **LD-2** is also found in the **heart** and **red blood cells**, though typically in lower concentrations than LD-1 in the heart. - It is often elevated after an MI, but typically LD-1 is elevated higher than LD-2 after an MI. *LD-5* - **LD-5** is predominantly found in the **liver** and **skeletal muscle**. - Its increase is indicative of liver damage or muscle injury, such as hepatitis or muscular dystrophy.
Question 84: What is the primary receptor for High-Density Lipoprotein (HDL) in cholesterol metabolism?
- A. SR-BI (Correct Answer)
- B. LDLR
- C. HDLR
- D. SR-82
Explanation: ***SR-BI*** - **Scavenger Receptor class B type 1 (SR-BI)** is the primary receptor responsible for selective uptake of **cholesteryl esters** from HDL into cells, particularly the liver and steroidogenic tissues. - Unlike other lipoprotein receptors, SR-BI mediates the **selective transfer** of cholesterol without internalizing the entire HDL particle. *LDLR* - The **Low-Density Lipoprotein Receptor (LDLR)** is the primary receptor for **LDL** and very low-density lipoprotein (VLDL) remnants, mediating their endocytosis and degradation. - While it plays a crucial role in cholesterol metabolism, its main function is related to the uptake of **LDL cholesterol**, not HDL. *HDLR* - **HDLR** is not a recognized receptor in cholesterol metabolism. - This term may be a distracter created by combining HDL with the common receptor nomenclature. *SR-82* - **SR-82** is not a recognized receptor involved in cholesterol metabolism. - Similar to HDLR, this is a distracter term.
Question 85: What is the primary role of calnexin and calreticulin in the endoplasmic reticulum?
- A. Degrade misfolded proteins
- B. Act as chaperones (Correct Answer)
- C. Serve as tumor markers
- D. Facilitate enzymatic reactions
Explanation: ***Act as chaperones*** - **Calnexin** and **calreticulin** are **chaperone proteins** located in the **endoplasmic reticulum (ER)**. - They bind to unfolded or misfolded glycoproteins to assist in their proper folding and assembly. - They are part of the **ER quality control system**, ensuring only properly folded proteins proceed to the Golgi apparatus. *Degrade misfolded proteins* - While misfolded proteins are eventually degraded through **ER-associated degradation (ERAD)**, this is not the primary function of calnexin and calreticulin. - These chaperones first attempt to **rescue and refold** proteins; degradation is a separate process involving other machinery. *Serve as tumor markers* - **Calnexin** and **calreticulin** are not typically used as **tumor markers** in clinical practice. - Their functions are related to protein quality control within the cell, not cancer detection. *Facilitate enzymatic reactions* - While some proteins in the ER are enzymes, **calnexin** and **calreticulin** themselves are not enzymes, nor do they primarily facilitate enzymatic reactions. - Their function is to ensure correct protein folding, distinct from direct catalytic activity.
Question 86: Which gene is responsible for the production of COX type 3?
- A. COX 3 gene
- B. COX 2 gene
- C. None of the above
- D. COX I gene (Correct Answer)
Explanation: ***COX I gene*** - COX-3 is an **alternatively spliced variant** of the **COX-1 gene** (specifically, a splice variant of the COX-1 mRNA that retains intron 1). - While it was initially thought to be a distinct gene, research has shown that it arises from the same genetic locus as COX-1. *COX 2 gene* - The COX-2 gene encodes for the **inducible cyclooxygenase enzyme**, which is responsible for prostaglandin synthesis during inflammation. - It is a separate gene from COX-1 and has distinct regulatory mechanisms and physiological roles. *COX 3 gene* - There is currently **no distinct gene in humans** specifically identified as "COX-3". - COX-3 refers to a protein isoform derived from the COX-1 gene, not a separate genetic locus. *None of the above* - This option is incorrect because COX-3 is indeed derived from the **COX-1 gene** through alternative splicing. - The existence of COX-3 as a distinct protein product has been demonstrated, although its precise physiological role in humans is still under investigation.
Question 87: Which of the following statements are true regarding the visual cycle cascade?
- A. All of the options are true (Correct Answer)
- B. Light causes isomerization of 11-cis-retinal to all-trans-retinal
- C. Retinal is involved in the visual cycle
- D. Involves a conformational change in opsin
Explanation: ***All of the statements are true*** The visual cycle cascade involves multiple interconnected events in phototransduction: **Light causes isomerization of 11-cis-retinal to all-trans-retinal** - This is the **primary photochemical event** that initiates vision - Light absorption causes the **cis-trans isomerization** in less than a picosecond - This conformational change is the only light-dependent step in the entire cascade **Retinal is involved in the visual cycle** - **11-cis-retinal** serves as the chromophore bound to opsin forming rhodopsin - After isomerization to **all-trans-retinal**, it must be converted back to 11-cis-retinal - This regeneration occurs through the **retinoid cycle** involving RPE cells **Involves a conformational change in opsin** - The isomerization of retinal triggers **conformational changes in opsin** - This converts rhodopsin to **metarhodopsin II** (the active form) - Activated opsin then activates **transducin** (G-protein), amplifying the signal and leading to hyperpolarization of photoreceptor cells All three statements accurately describe essential components of the visual cycle cascade.
Question 88: Which of the following proteins is primarily responsible for marking other proteins for degradation?
- A. Ubiquitin (Correct Answer)
- B. RNAse
- C. Zymase
- D. Chaperone
Explanation: **Ubiquitin** - **Ubiquitin** is a small regulatory protein that marks proteins for degradation by targeting them to the **proteasome**. - The ubiquitination process involves a cascade of enzymes (E1, E2, E3) that sequentially attach ubiquitin to the target protein, forming a **polyubiquitin chain**. *RNAse* - **RNAse** (Ribonuclease) is an enzyme that catalyzes the degradation of **RNA into smaller components**. - Its primary function is in **RNA processing** and turnover, not protein degradation. *Zymase* - **Zymase** is a complex of enzymes that catalyzes the **fermentation of sugar into ethanol and carbon dioxide**. - It is commonly found in yeast and is essential for **alcoholic fermentation**, with no role in protein degradation. *Chaperone* - **Chaperone proteins** assist in the **folding of newly synthesized proteins** and the refolding of misfolded or denatured proteins. - Their role is to ensure proper protein structure and function, preventing aggregation, rather than marking proteins for destruction.
Question 89: GlcNAc-P-P-oligosaccharide is -
- A. Proteoglycan
- B. Glycoprotein (Correct Answer)
- C. Collagen
- D. Phospholipid
Explanation: ***Glycoprotein*** - **GlcNAc-P-P-oligosaccharide** refers to the **N-linked oligosaccharide precursor** that is synthesized on a **dolichol pyrophosphate** carrier (`-P-P`). This complex is characteristic of the initial stages of **N-linked glycosylation**, a process that forms glycoproteins. - **N-acetylglucosamine (GlcNAc)** is a crucial sugar residue found at the reducing end of this precursor, linking it to the dolichol carrier. *Proteoglycan* - Proteoglycans consist of a **core protein** covalently attached to long, unbranched **glycosaminoglycan (GAG)** chains, such as chondroitin sulfate or heparin. - While they contain sugar units, their structure and synthesis pathway are distinct from the GlcNAc-P-P-oligosaccharide described, which is specific to N-linked glycoprotein synthesis. *Collagen* - **Collagen** is a fibrous protein, primarily composed of a triple helix of polypeptide chains rich in **glycine, proline, and hydroxyproline**. - Although collagen undergoes some post-translational modifications like **glycosylation**, it does not involve the GlcNAc-P-P-oligosaccharide precursor in its typical synthesis. *Phospholipid* - **Phospholipids** are a major component of cell membranes, composed of a **hydrophilic head** (containing a phosphate group) and two **hydrophobic fatty acid tails**. - They are lipids and do not contain carbohydrate structures like GlcNAc-P-P-oligosaccharide.
Question 90: Prolyl hydroxylase requires which cofactor?
- A. Vitamin C (Correct Answer)
- B. Iron (Fe²⁺)
- C. Molybdenum
- D. Vitamin K1
Explanation: ***Vitamin C*** - **Prolyl hydroxylase** is an enzyme critical for the hydroxylation of proline residues during **collagen synthesis**. - **Vitamin C** (ascorbic acid) acts as an essential **cofactor**, reducing the ferric iron of the enzyme back to its ferrous state after each catalytic cycle, enabling continued activity. - The enzyme requires both **iron (Fe²⁺)** as a metal cofactor and **vitamin C** to maintain the iron in its reduced state. *Iron (Fe²⁺)* - While **iron** is indeed required by prolyl hydroxylase as a **metal cofactor**, the question asks for the cofactor, which specifically refers to **vitamin C**. - Iron functions as part of the enzyme's active site, but vitamin C is the reducing agent that keeps iron functional. - Vitamin C deficiency (scurvy) leads to defective collagen synthesis despite adequate iron. *Molybdenum* - **Molybdenum** is a cofactor for several human enzymes, including **xanthine oxidase** and **sulfite oxidase**. - However, it plays no direct role in the activity of prolyl hydroxylase. *Vitamin K1* - **Vitamin K1** is a crucial cofactor for **gamma-glutamyl carboxylase**, an enzyme involved in the carboxylation of glutamic acid residues in clotting factors. - It is not involved in the hydroxylation of proline by prolyl hydroxylase.