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Reduction of disulfide bonds in peptides and proteins. Reduction des groupes disulfure dans les peptides et proteines

Conference:

Abstract

We have re-examined the mechanism of disulfide bond reduction in oxidized glutathione by C0[sub 2][sup .-] free radicals. The process appears to be a chain reaction whose initial yield depends on pH and on both peptide and formate ion concentrations, but remains independent on the radiation dose rate. Kinetic schemes drawn from studies on dithiothreitol are unable to account for the results obtained with glutathione and proteins, although the disulfide radical anion is the primary intermediate found with all compounds. The rate constant for its formation from C0[sub 2][sup .-] and glutathione is in the same range as those found using proteins, while decay pathways are somewhat different. Hypotheses are proposed to account for these differences. 6 figs., 2 tabs.
Authors:
Conte, D; [1]  Houee-Levin, C [2] 
  1. Institut Curie, 75 - Paris (France)
  2. Paris-5 Univ., 75 (France)
Publication Date:
Apr 01, 1993
Product Type:
Conference
Report Number:
CONF-9205369-
Reference Number:
AIX-24-066408; EDB-93-128779
Resource Relation:
Journal Name: Journal de Chimie Physique et de Physico-Chimie Biologique; (France); Journal Volume: 90:4; Conference: Meeting on radiation chemistry, Journees d'etudes sur la chimie des rayonnements, La Baume-les-Aix (France), 17-22 May 1992
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; GLUTATHIONE; REDUCTION; CHEMICAL REACTION KINETICS; CHEMICAL REACTION YIELD; DISULFIDES; GAMMA RADIATION; PH VALUE; RADICALS; RADIOLYSIS; CHEMICAL RADIATION EFFECTS; CHEMICAL REACTIONS; DECOMPOSITION; DRUGS; ELECTROMAGNETIC RADIATION; IONIZING RADIATIONS; KINETICS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; PEPTIDES; POLYPEPTIDES; PROTEINS; RADIATION EFFECTS; RADIATIONS; RADIOPROTECTIVE SUBSTANCES; REACTION KINETICS; YIELDS; 560120* - Radiation Effects on Biochemicals, Cells, & Tissue Culture
OSTI ID:
6398143
Country of Origin:
France
Language:
French
Other Identifying Numbers:
Journal ID: ISSN 0021-7689; CODEN: JCPBAN
Submitting Site:
FRN
Size:
Pages: 971-984
Announcement Date:
May 13, 2001

Conference:

Citation Formats

Conte, D, and Houee-Levin, C. Reduction of disulfide bonds in peptides and proteins. Reduction des groupes disulfure dans les peptides et proteines. France: N. p., 1993. Web.
Conte, D, & Houee-Levin, C. Reduction of disulfide bonds in peptides and proteins. Reduction des groupes disulfure dans les peptides et proteines. France.
Conte, D, and Houee-Levin, C. 1993. "Reduction of disulfide bonds in peptides and proteins. Reduction des groupes disulfure dans les peptides et proteines." France.
@misc{etde_6398143,
title = {Reduction of disulfide bonds in peptides and proteins. Reduction des groupes disulfure dans les peptides et proteines}
author = {Conte, D, and Houee-Levin, C}
abstractNote = {We have re-examined the mechanism of disulfide bond reduction in oxidized glutathione by C0[sub 2][sup .-] free radicals. The process appears to be a chain reaction whose initial yield depends on pH and on both peptide and formate ion concentrations, but remains independent on the radiation dose rate. Kinetic schemes drawn from studies on dithiothreitol are unable to account for the results obtained with glutathione and proteins, although the disulfide radical anion is the primary intermediate found with all compounds. The rate constant for its formation from C0[sub 2][sup .-] and glutathione is in the same range as those found using proteins, while decay pathways are somewhat different. Hypotheses are proposed to account for these differences. 6 figs., 2 tabs.}
journal = {Journal de Chimie Physique et de Physico-Chimie Biologique; (France)}
volume = {90:4}
place = {France}
year = {1993}
month = {Apr}
}