Organic Chemistry (9th Edition)
Organic Chemistry (9th Edition)
9th Edition
ISBN: 9780321971371
Author: Leroy G. Wade, Jan W. Simek
Publisher: PEARSON
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Chapter 24, Problem 24.43SP

(a)

Interpretation Introduction

To determine: The structure for glutathione that is consistent with the given information and the reason corresponding to the fact that glutathione fails to give a normal product from Edmann degradation, even though it gives a normal product from the Sanger reagent followed by hydrolysis.

Interpretation: The structure for glutathione that is consistent with the given information is to be shown and the reason corresponding to the fact that glutathione fails to give a normal product from Edmann degradation, even though it gives a normal product from the Sanger reagent followed by hydrolysis is to be stated.

Concept introduction: The process in which a proper series of amino acids is maintained peptide chain is known as Edmann degradation. This process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. The peptide bonds between other amino acids do not get disturb during this process.

(b)

Interpretation Introduction

To determine: The structure for glutathione disulphide that is formed by oxidation of glutathione and the balanced r-equation for the reaction of glutathione with hydrogen peroxide.

Interpretation: The structure for glutathione disulphide that is formed by oxidation of glutathione and the balanced equation for the reaction of glutathione with hydrogen peroxide are to be predicted.

Concept introduction: The process in which a proper series of amino acids is maintained peptide chain is known as Edmann degradation. This process includes the labelling of terminal amino residue followed by the cleavage of this terminal amino residue from the peptide chain. The peptide bonds between other amino acids do not get disturb during this process.

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Glutathione (GSH) is a tripeptide that serves as a mild reducing agent to detoxify peroxides and maintain the cysteineresidues of hemoglobin and other red blood cell proteins in the reduced state. Complete hydrolysis of glutathione givesGly, Glu, and Cys. Treatment of glutathione with carboxypeptidase gives glycine as the first free amino acid released.Treatment of glutathione with 2,4-dinitrofluorobenzene (Sanger reagent, Problem 24-21, page 1246), followed bycomplete hydrolysis, gives the 2,4-dinitrophenyl derivative of glutamic acid. Treatment of glutathione with phenylisothiocyanate does not give a recognizable phenylthiohydantoin, however.(a) Propose a structure for glutathione consistent with this information. Why would glutathione fail to give a normalproduct from Edman degradation, even though it gives a normal product from the Sanger reagent followed byhydrolysis?(b) Oxidation of glutathione forms glutathione disulfide (GSSG). Propose a structure for glutathione disulfide, and…
A nonapeptide released by globulins in the blood in response to a waspsting. Hydrolysis gives the following amino acids: 2 Arg, Gly, 2 Phe, 3 Pro, and Ser.Edman degradation gives phenylthiohydantoin of Arg. Cleavage with carboxypeptidase gives Arg. Partial hydrolysis gives the following di- and tripeptides: Phe-Ser, Pro-GlyPhe, Pro-Pro, Ser-Pro-Phe, Phe-Arg, and Arg-Pro. What is the amino acid sequence of this peptide?
Bradykinin is a linear nonapeptide released by blood plasma globulin in response to a wasp sting. It is a very potent pain-causing agent. Its constituent amino acids are 2R, G, 2F, 3P, S. The sue of 2,4-dinitrofluorobenzene and carboxypeptidase shows that both terminal residues are arginine. Partial hydrolysis of bradykinin gives the following di- and tripeptides: FS + PGF +PP + SPF + FR + RP

Chapter 24 Solutions

Organic Chemistry (9th Edition)

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