SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
SAPLINGPLUS F/BIOCHEM+ICLICKER REEF-CODE
9th Edition
ISBN: 9781319398583
Author: BERG
Publisher: MAC HIGHER
Question
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Chapter 7, Problem 2P
Interpretation Introduction

(a)

Interpretation:

The weight of the hemoglobin contained in an average red cell is to be stated.

Concept introduction:

Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.

Interpretation Introduction

(b)

Interpretation:

The total number of hemoglobin molecules present in an average red cell is to be stated.

Concept introduction:

Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.

Interpretation Introduction

(c)

Interpretation:

Whether the hemoglobin concentration in the red cells can be much higher than the observed value or not is to be stated.

Concept introduction:

Proteins are the biomolecules which are composed of the long chain of amino acid residues. The protein which contains oxygen and is present in the red blood cells in the body is known as hemoglobin. It contains iron as well.

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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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