SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
9th Edition
ISBN: 9781319398583
Author: BERG
Publisher: MAC HIGHER
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Chapter 11, Problem 38P
Interpretation Introduction

(a)

Interpretation:

The reason for the measurement of aggrecan degradation by the release of glycosaminoglycan needs to be explained.

Concept introduction:

The carbohydrates are combined with the proteins. Enzyme behaves aggrecan and produces a molecule.Some destruction can observe by the aggrecan.

Interpretation Introduction

(b)

Interpretation:

The reason for the glycosaminoglycan release to not indicate the aggrecan degradation needs to be explained.

Concept introduction:

Glycosaminoglycan is also known as mucopolysaccharides which have a series of disaccharides. This series contains amino sugar and uronic sugar. Glycosaminoglycan is also written as GAGs.

Interpretation Introduction

(c)

Interpretation:

The purpose of the control needs to be explained.

Concept introduction:

Enzyme behaves aggrecan and producesa molecule. Some destruction can observe by the aggrecan.

Interpretation Introduction

(d)

Interpretation:

The effect of adding IL-2 needs to be explained.

Concept introduction:

IL-2 is also known as interleukin which is a signaling molecule of the immune system.

Interpretation Introduction

(e)

Interpretation:

The response of aggrecanase inhibitor when IL-2 is added needs to be explained.

Concept introduction:

IL-2 is also known as interleukin which is a signaling molecule of the immune system.

Interpretation Introduction

(f)

Interpretation:

The reason for aggrecan destruction in the control needs to be explained.

Concept introduction:

Enzyme behaves aggrecan and produces a molecule. Some destruction can observe by the aggrecan.

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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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