Which condition may benefit from branched chain amino acids (leucine, isoleucine, and valine)?

Correct Answer: A

Rationale: Branched chain amino acids, such as leucine, isoleucine, and valine, are essential in preventing muscle breakdown. Therefore, they may be particularly important for a patient with cancer-related malnutrition, where maintaining muscle mass is crucial. Marasmus is a severe form of malnutrition characterized by energy deficiency, not specifically related to cancer. Cardiovascular disease and severe depression do not have a direct correlation with the need for branched chain amino acids to prevent muscle breakdown.

Correct Answer: B

Rationale: Cholecystokinin (CCK) is the correct answer. It is the hormone responsible for stimulating the gallbladder to contract and release bile to aid in fat digestion. Gastric lipase (Choice A) is an enzyme that breaks down fats in the stomach, not a hormone involved in gallbladder function. Vitamin D (Choice C) is important for calcium absorption and bone health, but it is not directly related to gallbladder function. Enterokinin (Choice D) is a peptide hormone that affects smooth muscle contractions in the gastrointestinal tract, but it is not specifically responsible for stimulating the gallbladder to release bile.

Correct Answer: C

Rationale: The correct answer is C: amino acids. Proteins are broken down by digestive enzymes into amino acids before being absorbed in the small intestine. Amino acids are the building blocks of proteins and are the form in which they are primarily absorbed. Choice A (fatty acids) is incorrect as fatty acids are the end products of fat digestion, not protein digestion. Choice B (disaccharides) is incorrect because disaccharides are sugars that are broken down into monosaccharides, not proteins. Choice D (polypeptides) is incorrect as proteins are broken down into amino acids and not absorbed as polypeptides.

Correct Answer: C

Rationale: Failed to generate a rationale of 500+ characters after 5 retries.

Correct Answer: D

Rationale: The correct answer is D: By enterokinase. Trypsin is activated by enterokinase, an enzyme secreted by the small intestine. Enterokinase plays a crucial role in converting trypsinogen into its active form, trypsin. Choices A, B, and C are incorrect because trypsin is specifically activated by enterokinase, not by zymogen, bile, or gastrin.

Correct Answer: D

Rationale: Negative nitrogen balance occurs when the body loses more nitrogen than it gains. This imbalance is often seen in conditions like anorexia in older adults, where insufficient protein intake leads to muscle breakdown and negative nitrogen balance. Choices A, B, and C do not typically lead to negative nitrogen balance as seen in anorexia in older adults.

Correct Answer: A

Rationale: The correct answer is 'tissue and plasma.' Protein turnover involves the continuous exchange of proteins between body tissues and the bloodstream (plasma) as part of normal metabolic processes. This process ensures a balance in protein levels throughout the body. Choices B, C, and D are incorrect as they do not represent the primary sites for protein turnover in the body.

Correct Answer: B

Rationale: Excessive intake of dietary protein can lead to impaired kidney function over time. Excessive protein consumption can put a strain on the kidneys as they work to eliminate the byproducts of protein metabolism. This can potentially lead to kidney damage. Choices A, C, and D are incorrect. Excessive protein intake is not directly linked to causing vitamin deficiencies, increasing weight loss, or decreasing the production of indispensable amino acids.

Correct Answer: C

Rationale: The correct answer is C, albumin. Albumin is a plasma protein that plays a crucial role in maintaining fluid balance in the blood. Collagen (choice A) is a structural protein found in connective tissues, not a plasma protein. Myosin (choice B) is a protein involved in muscle contraction, not found in the blood plasma. Phospholipid (choice D) is a type of lipid molecule, not a protein present in plasma.