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SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS

Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a pH so low that practically none of the SH groups of...

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Detalles Bibliográficos
Autores principales: Mirsky, A. E., Anson, M. L.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1936
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141444/
https://www.ncbi.nlm.nih.gov/pubmed/19872940
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author Mirsky, A. E.
Anson, M. L.
author_facet Mirsky, A. E.
Anson, M. L.
author_sort Mirsky, A. E.
collection PubMed
description Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a pH so low that practically none of the SH groups of native hemoglobin and of native lens protein are active. The effect of denaturation on the SH groups of a protein is to extend towards the acid side the pH range of their activity. It is possible to oxidize the iron-porphyrin and the SH groups of hemoglobin independently of each other.
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spelling pubmed-21414442008-04-23 SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS Mirsky, A. E. Anson, M. L. J Gen Physiol Article Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a pH so low that practically none of the SH groups of native hemoglobin and of native lens protein are active. The effect of denaturation on the SH groups of a protein is to extend towards the acid side the pH range of their activity. It is possible to oxidize the iron-porphyrin and the SH groups of hemoglobin independently of each other. The Rockefeller University Press 1936-01-20 /pmc/articles/PMC2141444/ /pubmed/19872940 Text en Copyright © Copyright, 1936, 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
Mirsky, A. E.
Anson, M. L.
SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title_full SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title_fullStr SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title_full_unstemmed SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title_short SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS : III. SULFHYDRYL GROUPS OF NATIVE PROTEINS—HEMOGLOBIN AND THE PROTEINS OF THE CRYSTALLINE LENS
title_sort sulfhydryl and disulfide groups of proteins : iii. sulfhydryl groups of native proteins—hemoglobin and the proteins of the crystalline lens
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141444/
https://www.ncbi.nlm.nih.gov/pubmed/19872940
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