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SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS

1. Cyanide inhibits the oxidation of the SH groups of cysteine and denatured egg albumin by the uric acid reagent. 2. At pH 4.8 cysteine is oxidized by the uric acid reagent and by ferricyanide in the presence but not in the absence of added copper sulfate. 3. In neutral solution, the uric acid reag...

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Autor principal: Anson, M. L.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1942
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142504/
https://www.ncbi.nlm.nih.gov/pubmed/19873279
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author Anson, M. L.
author_facet Anson, M. L.
author_sort Anson, M. L.
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description 1. Cyanide inhibits the oxidation of the SH groups of cysteine and denatured egg albumin by the uric acid reagent. 2. At pH 4.8 cysteine is oxidized by the uric acid reagent and by ferricyanide in the presence but not in the absence of added copper sulfate. 3. In neutral solution, the uric acid reagent oxidizes the SH groups of denatured egg albumin in the presence of urea but not in the presence of alkyl sulfate or in the absence of denaturing agents. 4. Ferricyanide oxidizes the SH groups of neutral denatured egg albumin even in the presence of alkyl sulfate or, if precautions are taken to avoid aggregation, in the absence of denaturing agents. 5. In acid solution, ferricyanide does not oxidize the SH groups of denatured egg albumin completely. The oxidation is more complete, however, in the presence of urea than in the presence of alkyl sulfate, and more complete in the presence of guanidine hydrochloride than in the presence of urea. 6. The uric acid reagent which does not oxidize the SH groups of neutral denatured but unhydrolyzed egg albumin in the absence of denaturing agents does, under the same conditions, oxidize the SH groups of egg albumin partially hydrolyzed by pepsin. 7. At pH 4.8 in alkyl sulfate solution ferricyanide oxidizes the SH groups of digested egg albumin more completely than the SH groups of denatured but undigested egg albumin.
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spelling pubmed-21425042008-04-23 SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS Anson, M. L. J Gen Physiol Article 1. Cyanide inhibits the oxidation of the SH groups of cysteine and denatured egg albumin by the uric acid reagent. 2. At pH 4.8 cysteine is oxidized by the uric acid reagent and by ferricyanide in the presence but not in the absence of added copper sulfate. 3. In neutral solution, the uric acid reagent oxidizes the SH groups of denatured egg albumin in the presence of urea but not in the presence of alkyl sulfate or in the absence of denaturing agents. 4. Ferricyanide oxidizes the SH groups of neutral denatured egg albumin even in the presence of alkyl sulfate or, if precautions are taken to avoid aggregation, in the absence of denaturing agents. 5. In acid solution, ferricyanide does not oxidize the SH groups of denatured egg albumin completely. The oxidation is more complete, however, in the presence of urea than in the presence of alkyl sulfate, and more complete in the presence of guanidine hydrochloride than in the presence of urea. 6. The uric acid reagent which does not oxidize the SH groups of neutral denatured but unhydrolyzed egg albumin in the absence of denaturing agents does, under the same conditions, oxidize the SH groups of egg albumin partially hydrolyzed by pepsin. 7. At pH 4.8 in alkyl sulfate solution ferricyanide oxidizes the SH groups of digested egg albumin more completely than the SH groups of denatured but undigested egg albumin. The Rockefeller University Press 1942-01-20 /pmc/articles/PMC2142504/ /pubmed/19873279 Text en Copyright © Copyright, 1942, by The Rockefeller Institute for Medical Research This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Anson, M. L.
SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title_full SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title_fullStr SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title_full_unstemmed SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title_short SOME FACTORS WHICH INFLUENCE THE OXIDATION OF SULFHYDRYL GROUPS
title_sort some factors which influence the oxidation of sulfhydryl groups
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142504/
https://www.ncbi.nlm.nih.gov/pubmed/19873279
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