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Q.1- What is the biological advantage of secretion of proteolytic enzymes  in the zymogen forms in the gut?

Q.2- What is the role played by Glutathione in the absorption of amino acids?

Q.3- Discuss the disorders associated with the absorption of amino acids.

Q.4- Justify the reasoning that glutamic acid plays a pivotal role in the metabolism of amino acids.

Q.5- Alpha Methyldopa is a drug used in the treatment of hypertension. Explain its possible mode of action.(Hint- It is an inhibitor of DOPA Decarboxylase enzyme)

Q.6- Discuss the mechanism by which Ammonia is detoxified in the body.

Q.7-Describe the glucose-alanine cycle and explain its role in amino acid metabolism.

Q.8-Decarboxylation of some amino acids can lead to synthesis of physiologically important compounds. Give evidences in support of this statement.

Q.9- What is the significance of urea cycle apart from urea formation?

Q.10- Give the reactions of the pathway of urea synthesis that involve the participation of ATP

Q.11-What is oxidative deamination of amino acids? Give examples in support of your answer.

Q.12-Name two neurotransmitters that are derived from the metabolism of amino acids Show by means of reactions the mechanism of synthesis of each of them.

Q.13- What is transdeamination? State its importance and illustrate the answer giving reactions in support of your answer.

 Q.14-Discuss the biochemical roles of glutamate and glutamine in cell metabolism

 Q.15-How will you define a non-essential amino acid? Under what condition can a non-essential amino acid become essential? Explain clearly and illustrate your answer giving suitable example.

Q.16-Discuss briefly about the metabolic role of Tyrosine,giving examples and suitable reactions

Q.17-Describe transmethylation reactions giving suitable examples

Q.18-Show, by means of a diagram, the relationship between the urea cycle and the citric acid cycle

Q.19-What is meant by (a) ketogenic amino acid and (b)glucogenic amino acid ? Illustrate your answer with a named example of each.

 Q.20-Explain why phenylketonurics are warned against eating products containing the artificial sweetener aspartame (Nutrasweet; chemical name L-Aspartyl-L-Phenylalanine methyl ester)?

 Q.21-Why are polyamines important in mammalian metabolism? Write the reactions of polyamine biosynthesis and catabolism

 Q.22-Describe the importance of glutamic acid in the synthesis and catabolism of other amino acids

 Q.23-Name the immediate precursor and the enzyme catalyzing the formation of: (a) GABA (gamma-amino butyric acid) (b) Histamine  and (c) DOPA(dihydroxyphenylalanine).

 Q.24-Explain briefly why ammonia is highly toxic to brain cells?

 Q.25-A diet containing very little phenylalanine is used in the treatment of Phenylketonuria, what is the reason? Explain why it is necessary to supplement tyrosine in this diet.

 Q.26-Certain amino acid are described as glucogenic. Explain briefly what is meant by the term “glucogenic”, illustrating your answer with the metabolic reactions of three named glucogenic amino acid.

 Q.27-Outline the metabolic processes by Tryptophan is converted into hormones and neurotransmitters. Describe briefly the clinical condition produced by deficiencies in these processes.

 Q.28-Discuss the significance of Xanthurenic acid excretion test.

 Q.29-Show by means of a diagram the point of entry of phenylalanine, glutamine and methionine into the citric acid cycle

 Q.30-Outline the steps of urea cycle and state its importance.

 Q.31-Give the reaction catalyzed by a named (a) amino acid Decarboxylase and (b) aminotransferase

 Q.32-What is the origin of the nitrogen atoms in urea formation ?  Discuss the reason that deficiency of urea cycle enzymes especially Ornithine Trans Carbamoylase leads to Orotic aciduria

 Q.33-What is the P:O ratio when glutamate is oxidized by the glutamate dehydrogenase reaction? Show the reaction insupport of your answer. 

 Q.34-Outline the metabolic role of glycine, justifying the fact that it is nutritionally non-essential but functionally very essential.

 Q.35-Trace the metabolic origin of the following urinary constituents: (a) creatinine (b) urea and (c) ammonia. Discuss the significance of their altered excretion with suitable examples.

Q.36-Account for the biochemical changes in the blood of a phenylketonuric subject.

Q.37- What is the biochemical basis for pellagra like rashes in Hart nup disease ?

Q.38- What is the defect in Carcinoid syndrome?  What is the biochemical basis of increased HIAA (Hydroxy Indole Acetic acid excretion) in Carcinoid syndrome ?

Q.39- Metabolism of which amino acid is associated with FIGLU excretion test for the detection of underlying folic acid deficiency?

Q.40- What is the defect in Maple syrup urine disease? Discuss in brief about the symptoms, laboratory diagnosis and its treatment.

Q.41- What is the cause of  increased risk for ischemic heart disease in patients of Homocystinuria  Discuss in brief about the classification, clinical manifestations and laboratory diagnosis of Homocystinuria.

Q.42- Discuss the functions and therapeutic uses of nitric oxide

Q.43–Discuss briefly about the biological and clinical significance of Transaminases.

 Q.44- What is the defect in Cystinuria? Why is it associated with renal stone formation?

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