What primarily forms the core of chylomicrons?
Which protein is responsible for conserving iron in the body?
Which of the following statements about Niemann-Pick disease is false?
Which protein does the domain of plasminogen resemble?
Which of the following stimulates Acetyl CoA Carboxylase?
Which of the following is an example of an exopeptidase?
Calcium absorption is hampered by
HDL is called good cholesterol because -
Amide group is present in which part of protein?
Which of the following statements are true regarding the visual cycle cascade?
NEET-PG 2015 - Biochemistry NEET-PG Practice Questions and MCQs
Question 31: What primarily forms the core of chylomicrons?
- A. Triglycerides and Cholesterol together
- B. Triglycerides (Correct Answer)
- C. Free fatty acids
- D. Triglyceride, Cholesterol and Phospholipids
Explanation: ***Triglycerides*** - Chylomicrons are primarily responsible for transporting **dietary triglycerides** from the intestines to other tissues. - Their large core, composed mainly of **triglycerides**, allows efficient transport of these hydrophobic molecules. *Triglycerides and Cholesterol together* - While **cholesterol** is present in chylomicrons, it is less abundant than **triglycerides** and primarily exists as **cholesterol esters** in the core. - The core is not an equal mixture; **triglycerides** overwhelmingly dominate the volume. *Free fatty acids* - **Free fatty acids** are transported in the blood primarily bound to **albumin**, not within the core of chylomicrons. - Chylomicrons typically carry **esterified fatty acids** as part of triglycerides. *Triglyceride, Cholesterol and Phospholipids* - **Phospholipids** form the outer monolayer of the chylomicron, along with apoproteins, making them **amphipathic**. - They do not constitute a core component but rather the **surface interface** with the aqueous environment.
Question 32: Which protein is responsible for conserving iron in the body?
- A. Ferritin (Correct Answer)
- B. Hepcidin
- C. Hemopexin
- D. Transferrin
Explanation: ***Ferritin*** - **Ferritin** is the primary intracellular protein that **conserves iron** in the body by storing it in a safe, non-toxic, and bioavailable form - It is found mainly in the liver, spleen, and bone marrow, serving as the body's **iron reserve** - When iron is abundant, ferritin stores it; when iron is needed, ferritin releases it, thus **conserving iron for future use** - Serum ferritin levels directly reflect total body iron stores *Hepcidin* - **Hepcidin** is a regulatory peptide hormone that controls iron homeostasis by inhibiting **ferroportin**, the iron export channel - It reduces iron absorption from the intestine and iron release from macrophages during inflammation or iron overload - While it regulates iron distribution, it is a hormone, not a storage protein, and does not directly conserve iron within cells *Hemopexin* - **Hemopexin** binds free **heme** in plasma, preventing oxidative damage and delivering it to the liver for catabolism - It helps recover iron from heme but does not store or conserve iron in the body *Transferrin* - **Transferrin** is a plasma protein that **transports iron** from absorption sites (intestine) and storage sites (liver, spleen) to tissues that need it - Its role is iron delivery, not conservation or storage
Question 33: Which of the following statements about Niemann-Pick disease is false?
- A. Due to deficiency of sphingomyelinase.
- B. CNS symptoms are present in type A.
- C. Type B Niemann-Pick disease is characterized by severe neurological symptoms. (Correct Answer)
- D. Histiocytes show PAS positive inclusions, and Type A is more severe.
Explanation: ***Type B Niemann-Pick disease is characterized by severe neurological symptoms.*** - This statement is **false** because **Type B Niemann-Pick disease** generally presents with **visceral involvement** (e.g., hepatosplenomegaly, lung disease) with **minimal to no neurological symptoms**. - **Severe neurological symptoms** are characteristic of **Type A Niemann-Pick disease**, which involves widespread CNS degeneration and a more rapidly progressive course. *Due to deficiency of sphingomyelinase.* - This statement is **true**. - Niemann-Pick disease (Types A and B) is caused by a deficiency of the enzyme **acid sphingomyelinase**, leading to the accumulation of sphingomyelin within lysosomes, particularly in macrophages. *CNS symptoms are present in type A.* - This statement is **true**. - **Type A Niemann-Pick disease** is the most severe form and is characterized by significant **neurodegeneration** in addition to visceral involvement. - Patients typically present with **developmental regression**, **ataxia**, and **spasticity** due to extensive sphingomyelin deposition in the central nervous system. *Histiocytes show PAS positive inclusions, and Type A is more severe.* - This statement is **true**. - The characteristic "foam cells" (lipid-laden macrophages/histiocytes) found in tissues of Niemann-Pick patients stain positive with **periodic acid–Schiff (PAS)** due to accumulated sphingomyelin. - **Type A Niemann-Pick disease** is indeed the most severe form, with a rapidly progressive course and early fatality, usually by early childhood.
Question 34: Which protein does the domain of plasminogen resemble?
- A. Fibrinogen (a clotting protein)
- B. LDL receptor (a lipid metabolism protein)
- C. Apolipoprotein (a) (a lipoprotein) (Correct Answer)
- D. Prothrombin (a coagulation protein)
Explanation: ***Apolipoprotein (a) (a lipoprotein)*** - **Plasminogen** and **apolipoprotein (a)** share structural homology, specifically due to the presence of **kringle domains**. - This structural similarity suggests a potential for apolipoprotein (a) to **interfere with plasminogen’s fibrinolytic activity**, contributing to **atherosclerosis**. *Fibrinogen (a clotting protein)* - While plasmin acts on fibrinogen (and its derivative fibrin), its domain structure does not **resemble fibrinogen**. - **Fibrinogen** is a large, multi-domain glycoprotein crucial for **clot formation**, distinct from plasminogen's primarily **kringle-rich structure**. *LDL receptor (a lipid metabolism protein)* - The **LDL receptor** is involved in **cholesterol uptake** by cells and has structural features like ligand-binding repeats and epidermal growth factor (EGF) repeats. - Its domain structure is **not similar to plasminogen**, which is characterized by **kringle domains** and a protease domain. *Prothrombin (a coagulation protein)* - **Prothrombin** is a precursor to thrombin, featuring **gla domains**, kringle-like domains (though structurally distinct from plasminogen's), and a serine protease domain. - While both are involved in coagulation/fibrinolysis, their **overall domain arrangements and specific kringle structures differ** significantly.
Question 35: Which of the following stimulates Acetyl CoA Carboxylase?
- A. Starvation
- B. Glucagon
- C. Citrate (Correct Answer)
- D. None of the options
Explanation: ***Citrate*** - **Citrate** is an allosteric activator of **Acetyl-CoA Carboxylase (ACC)**, indicating abundant energy and precursor availability for fatty acid synthesis. - This activation promotes the conversion of **Acetyl-CoA** to **Malonyl-CoA**, the committed step in **fatty acid synthesis**. *Starvation* - **Starvation** leads to energy deficit, which generally **inhibits** anabolic processes like fatty acid synthesis. - In this state, enzymes involved in anabolic pathways are often downregulated or inhibited to conserve energy. *Glucagon* - **Glucagon** is a hormone that signals low blood glucose and promotes catabolic processes such as **glycogenolysis** and **gluconeogenesis**. - It **inhibits** fatty acid synthesis by phosphorylating and inactivating **Acetyl-CoA Carboxylase**, thus opposing citrate's activating effect. *None of the options* - **Citrate** is a known stimulator of Acetyl CoA Carboxylase. - This option is incorrect because there is a correct answer among the choices.
Question 36: Which of the following is an example of an exopeptidase?
- A. Trypsin
- B. Chymotrypsin
- C. Elastase
- D. Carboxypeptidases (Correct Answer)
Explanation: ***Carboxypeptidases*** - **Carboxypeptidases** are enzymes that cleave the **C-terminal** (carboxyl end) amino acid from a polypeptide chain, making them a type of exopeptidase. - They are crucial in protein digestion, releasing individual amino acids from the end of protein chains. *Trypsin* - **Trypsin** is an **endopeptidase** that cleaves peptide bonds within protein chains, specifically at the carboxyl side of **lysine** or **arginine** residues. - It does not cleave amino acids from the ends of polypeptide chains. *Chymotrypsin* - **Chymotrypsin** is an **endopeptidase** that cleaves peptide bonds within a polypeptide chain, primarily at the carboxyl side of **tyrosine**, **tryptophan**, or **phenylalanine**. - Its action is internal to the protein sequence, not at the termini. *Elastase* - **Elastase** is also an **endopeptidase** that cleaves peptide bonds internally, specifically targeting small, uncharged amino acid residues like **alanine**, **glycine**, and **valine**. - Its primary role is to break down elastin, an elastic protein in connective tissues, but it does so by internal cleavage.
Question 37: Calcium absorption is hampered by
- A. Protein
- B. Lactose
- C. Acid
- D. Phytates (Correct Answer)
Explanation: ***Phytates*** - **Phytates** (phytic acid) found in whole grains, legumes, nuts, and seeds bind to calcium, forming an insoluble complex that significantly **reduces its absorption** in the intestines. - This binding prevents the free calcium ions from crossing the intestinal wall into the bloodstream. *Protein* - **Protein** generally *enhances* calcium absorption, especially when consumed in moderate amounts, as some amino acids can form soluble calcium complexes. - However, very high protein intake, particularly from animal sources, *may* slightly increase urinary calcium excretion in the long term, but it does not directly hamper intestinal absorption. *Lactose* - **Lactose**, a sugar found in milk, is known to *enhance* calcium absorption. - It does so by creating a more acidic environment in the small intestine and by forming soluble complexes with calcium, making it more bioavailable. *Acid* - **Stomach acid** (hydrochloric acid) is crucial for calcium absorption as it helps to solubilize calcium salts from food. - A *reduced* acidic environment, such as from antacid use or certain medical conditions, would hamper calcium absorption, but acid itself is beneficial.
Question 38: HDL is called good cholesterol because -
- A. Removes cholesterol from peripheral tissues (Correct Answer)
- B. Increases cholesterol delivery to peripheral tissues
- C. Stimulates cholesterol synthesis in the liver
- D. Activates enzymes that break down triglycerides
Explanation: ***Removes cholesterol from peripheral tissues*** - **High-density lipoprotein (HDL)** is known as "good cholesterol" due to its role in **reverse cholesterol transport**, a process where it collects excess cholesterol from peripheral cells and tissues. - This action helps to prevent the accumulation of cholesterol in arteries, thereby reducing the risk of **atherosclerosis** and cardiovascular disease. - HDL then transports this cholesterol to the liver for excretion via bile, completing the protective cycle. *Increases cholesterol delivery to peripheral tissues* - This is actually the opposite of HDL's function and describes the role of **LDL (low-density lipoprotein)**, which is considered "bad cholesterol." - LDL delivers cholesterol to peripheral tissues, and excess LDL can lead to **atherosclerotic plaque formation**. *Stimulates cholesterol synthesis in the liver* - HDL does not directly stimulate cholesterol synthesis in the liver; rather, its role is primarily in **cholesterol efflux** from cells and transport. - The liver's cholesterol synthesis is regulated by various factors, including dietary intake and cellular cholesterol levels via the **SREBP pathway**, but HDL does not upregulate hepatic cholesterol synthesis. *Activates enzymes that break down triglycerides* - While HDL does activate **LCAT (lecithin-cholesterol acyltransferase)** for cholesterol esterification, its primary "good" function is not the breakdown of triglycerides. - **Lipoprotein lipase (LPL)** is the primary enzyme responsible for triglyceride breakdown in lipoproteins like VLDL and chylomicrons.
Question 39: Amide group is present in which part of protein?
- A. Amino-terminal
- B. Peptide bond (Correct Answer)
- C. Disulfide bond
- D. Carboxy-terminal
Explanation: ***Peptide bond*** - A **peptide bond** is formed between the **carboxyl group** of one amino acid and the **amino group** of another, releasing a water molecule. This bond has an **amide structure**. - The repeated formation of these amide (peptide) bonds links amino acids into long chains, forming a **polypeptide** or protein. *Amino-terminal* - The **amino-terminal (N-terminal)** end of a protein contains a free **amino group (-NH2)**, which is not part of an amide linkage within the polypeptide backbone. - It marks the beginning of the polypeptide chain and is typically involved in various cellular interactions and modifications. *Disulfide bond* - A **disulfide bond** is a covalent bond formed between two **sulfhydryl groups (-SH)** of **cysteine residues**, leading to the formation of a **cystine** residue. - This bond is crucial for stabilizing the **tertiary and quaternary structures** of proteins, but it does not contain an amide group. *Carboxy-terminal* - The **carboxy-terminal (C-terminal)** end of a protein contains a free **carboxyl group (-COOH)**, which is not part of an amide linkage within the polypeptide backbone. - It marks the end of the polypeptide chain and plays roles in protein processing, targeting, and regulation.
Question 40: 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.