BIOCHEMISTRY
BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
Question
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Chapter 27, Problem 30P
Interpretation Introduction

(a)

Interpretation:

The effect of excess insulin on lipid metabolism should be determined.

Concept introduction:

Insulin is a type of anabolic hormone which is produced and secreted by islets cells of the pancreas. The main function of insulin is to control the blood glucose level in the body. It prevents the high glucose level (hyperglycemia) and low blood glucose level (hypoglycemia).

Interpretation Introduction

(b)

Interpretation:

The effect of insulin on protein metabolism.

Concept introduction:

Insulin is a type of anabolic hormone which is produced and secreted by islets cells of the pancreas. The main function of insulin is to control the blood glucose level in the body. It prevents the high glucose level (hyperglycemia) and low blood glucose level (hypoglycemia).

Interpretation Introduction

(c)

Interpretation:

The biochemical basis for the distended bellies of children suffering from kwashiorkor should be determined.

Concept introduction:

Insulin is a type of anabolic hormone, which is produced and secreted by islets cells of the pancreas. The main function of insulin is to control the blood glucose level in the body. It prevents the high glucose level (hyperglycemia) and low blood glucose level (hypoglycemia).

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Students have asked these similar questions
The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism  of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help
To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?
To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.  Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!
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