What is the primary reason for the detergent action of bile salts?
Glucagon stimulates
What is the unit for a prolactin level of 20 in blood?
Which of the following is not an androgen?
Carbonic anhydrase activity is found in all of the following except?
What is the approximate half-life of albumin in the human body?
What is the half-life of Prealbumin?
Which of the following is activated by calmodulin?
Which of the following statements about G protein-coupled receptors (GPCRs) is true?
In type IA Maple Syrup Urine Disease, which gene mutation is responsible?
NEET-PG 2013 - Biochemistry NEET-PG Practice Questions and MCQs
Question 21: What is the primary reason for the detergent action of bile salts?
- A. Hydrophobic properties
- B. Acts as a zwitterion
- C. Amphipathic nature (Correct Answer)
- D. None of the options
Explanation: ***Amphipathic nature*** - Bile salts are **amphipathic molecules**, meaning they have both **hydrophilic (water-loving)** and **hydrophobic (water-fearing)** regions. - This dual nature allows them to emulsify fats by surrounding lipid droplets with their hydrophobic ends dissolving in the fat and their hydrophilic ends facing the aqueous environment, stabilizing the emulsion. *Hydrophobic properties* - While bile salts do possess **hydrophobic regions**, these alone are not sufficient for detergent action. - The ability to interact with both oil and water phases simultaneously is crucial for their role in **emulsification**. *Acts as a zwitterion* - A zwitterion is a molecule with both a **positive and negative charge**, but an overall neutral charge. - This property is not the primary mechanism behind the **detergent action** of bile salts, which relies more on their ability to solubilize fats. *None of the options* - The **amphipathic nature** is indeed the primary reason for the detergent action; therefore, this option is incorrect.
Question 22: Glucagon stimulates
- A. Gluconeogenesis (Correct Answer)
- B. Glycogenesis
- C. Fatty acid synthesis
- D. Glycolysis
Explanation: ***Gluconeogenesis*** - **Glucagon** is a hormone that primarily acts to raise **blood glucose levels** by stimulating the production of glucose from non-carbohydrate sources. - This process, **gluconeogenesis**, occurs mainly in the liver and is initiated by glucagon to counteract hypoglycemia. *Glycogenesis* - **Glycogenesis** is the process of synthesizing **glycogen** from glucose and is primarily stimulated by insulin when blood glucose levels are high. - Glucagon's role is to *inhibit* glycogen synthesis and instead promote glycogen breakdown. *Fatty acid synthesis* - **Fatty acid synthesis** is an anabolic process that primarily occurs when there is an excess of energy and glucose, often stimulated by **insulin**. - Glucagon generally has an **inhibitory effect** on fatty acid synthesis, as its main goal is to mobilize energy stores, not create them. *Glycolysis* - **Glycolysis** is the breakdown of glucose to produce energy, and it is stimulated when glucose is abundant and energy is needed. - Glucagon primarily acts to *inhibit* glycolysis in the liver, thereby conserving glucose for use by other tissues and promoting its release into the bloodstream.
Question 23: What is the unit for a prolactin level of 20 in blood?
- A. ng/ml (Correct Answer)
- B. mg/ml
- C. mg/l
- D. ng/l
Explanation: ***ng/ml*** - Prolactin levels in blood are typically measured in **nanograms per milliliter (ng/mL)**, reflecting the very small concentrations of hormones. - A value of 20 ng/mL falls within the typical reference range for prolactin. *mg/mL* - **Milligrams per milliliter (mg/mL)** is a unit used for much higher concentrations, more common for drugs or larger molecules, not hormones like prolactin. - If prolactin were measured in mg/mL, a value of 20 mg/mL would be an astronomically high and physiologically impossible level. *mg/L* - **Milligrams per liter (mg/L)** is also a unit for higher concentrations than those typically seen for hormones in blood. - 20 mg/L is equivalent to 20 µg/mL or 20,000 ng/mL, which would indicate severe hyperprolactinemia. *ng/L* - **Nanograms per liter (ng/L)** is a unit for extremely low concentrations. - A reading of 20 ng/L would be too low for normal physiological prolactin levels, as 1 ng/mL equals 1000 ng/L.
Question 24: Which of the following is not an androgen?
- A. 17α-hydroxyprogesterone (Correct Answer)
- B. Testosterone
- C. Dihydrotestosterone
- D. Androstenedione
Explanation: ***17α-hydroxyprogesterone*** - This is a **progesterone derivative** and an intermediate in the synthesis of androgens and corticosteroids, but it does **not possess significant androgenic activity** itself. - Its primary role is as a precursor, rather than a direct androgen. *Testosterone* - **Testosterone** is the **primary male sex hormone** and a potent androgen, responsible for the development of male secondary sexual characteristics. - It plays crucial roles in muscle mass, bone density, libido, and erythropoiesis. *Dihydrotestosterone* - **Dihydrotestosterone (DHT)** is a potent androgen, formed from testosterone by the enzyme 5α-reductase. - DHT is responsible for the development of external male genitalia during fetal development and contributes to prostate growth and male pattern baldness in adults. *Androstenedione* - **Androstenedione** is a **weak androgen** and an important **precursor hormone** in the biosynthesis of testosterone and estrogens. - It is produced in the adrenal glands and gonads, serving as an intermediate step in steroidogenesis.
Question 25: Carbonic anhydrase activity is found in all of the following except?
- A. Brain
- B. Kidney
- C. RBC
- D. Plasma (Correct Answer)
Explanation: ***Plasma*** - **Carbonic anhydrase** is an intracellular enzyme that catalyzes the rapid interconversion of carbon dioxide and water to carbonic acid, **bicarbonate**, and protons. - It is notably **absent in plasma** in healthy individuals, as it is primarily found within cells where its function is crucial for pH regulation and CO2 transport. *Brain* - Carbonic anhydrase is found in various brain cells, including **neurons**, **oligodendrocytes**, and **astrocytes**. - It plays a vital role in pH regulation, fluid balance, and the production of cerebrospinal fluid (CSF) within the **central nervous system**. *Kidney* - The kidney is rich in carbonic anhydrase, particularly in the **proximal tubules** and collecting ducts. - It is critical for **bicarbonate reabsorption** and proton excretion, essential processes for maintaining acid-base balance. *RBC* - **Red blood cells (RBCs)** contain a high concentration of carbonic anhydrase (specifically CA-I and CA-II isoforms). - This enzyme facilitates the rapid conversion of CO2 to bicarbonate for transport to the lungs and the reverse reaction for **CO2 exhalation**.
Question 26: What is the approximate half-life of albumin in the human body?
- A. 30 days
- B. 20 days (Correct Answer)
- C. 3 days
- D. 7 days
Explanation: ***20 days*** - The **half-life of albumin** in the human body is approximately **20 days**, reflecting the time it takes for half of the circulating albumin to be catabolized or excreted. - This relatively long half-life means that changes in albumin levels, such as those due to malnutrition or liver disease, may take several weeks to become evident. *3 days* - A half-life of 3 days is too short for albumin, which is a major, long-lasting plasma protein. - Proteins with such a short half-life typically include more rapidly turnover proteins or small peptides. *7 days* - A half-life of 7 days is also too short for albumin, which plays a critical role in maintaining plasma oncotic pressure and transporting various substances. - While some proteins have a 7-day half-life, albumin's is considerably longer. *30 days* - A half-life of 30 days is longer than the typical half-life of albumin. - While some proteins may have half-lives in this range, 20 days is the more commonly accepted value for albumin.
Question 27: What is the half-life of Prealbumin?
- A. 2 days (Correct Answer)
- B. 10 days
- C. 20 days
- D. 40 days
Explanation: ***2 days*** - Prealbumin, also known as transthyretin, has a **short half-life** of approximately 2-3 days, making it a sensitive indicator of recent changes in **nutritional status**. - Its rapid turnover allows for prompt reflection of improvement or deterioration in protein synthesis. *10 days* - A half-life of 10 days would make prealbumin less responsive to acute changes in nutrition compared to its actual turnover rate. - This duration is longer than the typical half-life of proteins used to monitor **short-term nutritional status**. *20 days* - A 20-day half-life would indicate a protein with a much slower turnover, unsuitable for monitoring **acute nutritional interventions**. - Proteins with such long half-lives, like **albumin**, reflect more chronic states rather than rapid changes. *40 days* - A half-life of 40 days is characteristic of proteins like **albumin**, which are influenced by longer-term nutritional and inflammatory processes. - Such a long half-life would not be useful for assessing immediate responses to **nutritional support** or acute disease states.
Question 28: Which of the following is activated by calmodulin?
- A. Muscle phosphorylase
- B. Calcium/calmodulin-dependent protein kinase (Correct Answer)
- C. Phospholipase C
- D. Adenylyl cyclase
Explanation: ***Calcium/calmodulin-dependent protein kinase*** - **Calmodulin** is a **calcium-binding messenger protein** that, when bound to calcium, undergoes a conformational change allowing it to activate various enzymes, including **calcium/calmodulin-dependent protein kinases** (CaMKs). - CaMKs play crucial roles in many cellular processes, including **metabolism**, **gene expression**, and **neurotransmission**, by phosphorylating target proteins. *Muscle phosphorylase* - **Muscle phosphorylase** (glycogen phosphorylase) is primarily activated by **epinephrine**, **AMP**, and **nerve stimulation** (via calcium), but not directly by calmodulin. - Its activation leads to the breakdown of **glycogen** into glucose-1-phosphate. *Phospholipase C* - **Phospholipase C (PLC)** is typically activated by **G protein-coupled receptors** and **tyrosine kinase receptors**, leading to the production of **inositol trisphosphate (IP3)** and **diacylglycerol (DAG)**. - While it plays a role in calcium signaling upstream (releasing calcium from stores), it is not directly activated by calmodulin. *Adenylyl cyclase* - **Adenylyl cyclase (AC)** is a key enzyme in generating **cyclic AMP (cAMP)**, and is commonly regulated by **G proteins** (specifically Gs and Gi subunits). - While certain isoforms (AC1, AC3, AC8) can be directly activated by calcium/calmodulin, **CaMK** remains the most classical and direct example of calmodulin activation.
Question 29: Which of the following statements about G protein-coupled receptors (GPCRs) is true?
- A. The three subunits alpha, beta, and gamma must remain together as a complex for G protein to function.
- B. G proteins can act as either inhibitory or excitatory based on the type of alpha subunit. (Correct Answer)
- C. G proteins bind directly to hormones to become activated.
- D. In the resting state, G proteins are bound to GTP.
Explanation: ***G proteins can act as either inhibitory or excitatory based on the type of alpha subunit.*** - Different classes of Gα subunits (e.g., **Gαs**, **Gαi**, **Gαq**) couple to diverse downstream effectors, leading to either **stimulation** (excitatory) or **inhibition** of cellular processes. - For example, **Gαs** activates adenylyl cyclase, while **Gαi** inhibits it, demonstrating their opposing roles. *The three subunits alpha, beta, and gamma must remain together as a complex for G protein to function.* - Upon activation, the **Gα subunit dissociates** from the **Gβγ dimer**, and both free units can then independently modulate effector molecules. - For the G protein to function in signal transduction, the α subunit often separates from the βγ dimer to interact with its target enzyme or ion channel. *G proteins bind directly to hormones to become activated.* - **GPCRs** (the receptors themselves) bind to hormones or other ligands on the **extracellular side** of the membrane. - The binding of the ligand to the GPCR induces a conformational change in the receptor, which then activates the associated G protein on the intracellular side. *In the resting state, G proteins are bound to GTP.* - In the **resting (inactive) state**, the Gα subunit of the trimeric G protein is bound to **GDP**. - Activation occurs when the GPCR facilitates the exchange of **GDP for GTP** on the Gα subunit.
Question 30: In type IA Maple Syrup Urine Disease, which gene mutation is responsible?
- A. BCKDHB
- B. DBT
- C. DLD
- D. BCKDHA (Correct Answer)
Explanation: ***BCKDHA*** - **Maple Syrup Urine Disease (MSUD)** type IA is caused by a mutation in the **BCKDHA gene**, which codes for the E1α subunit of the **branched-chain α-keto acid dehydrogenase (BCKD) complex**. - This **enzyme complex** is crucial for the metabolism of **branched-chain amino acids (BCAAs)**: leucine, isoleucine, and valine. *BCKDHB* - The **BCKDHB gene** codes for the E1β subunit of the **BCKD complex**. - Mutations in **BCKDHB** are associated with **type IB MSUD**, not type IA. *DBT* - The **DBT gene** codes for the E2 subunit (dihydrolipoyl transacylase) of the **BCKD complex**. - Mutations in **DBT** are responsible for **type II MSUD**. *DLD* - The **DLD gene** codes for the E3 subunit (dihydrolipoyl dehydrogenase), which is a component shared by several **α-keto acid dehydrogenase complexes**. - Mutations in the **DLD gene** lead to **type III MSUD** and other pyruvate dehydrogenase complex deficiencies, rather than type IA.