Cargando…
SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN
1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p (50)). Mersalyl and mercuric chloride...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1956
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147547/ https://www.ncbi.nlm.nih.gov/pubmed/13295556 |
_version_ | 1782144465143595008 |
---|---|
author | Riggs, Austen F. Wolbach, Robert A. |
author_facet | Riggs, Austen F. Wolbach, Robert A. |
author_sort | Riggs, Austen F. |
collection | PubMed |
description | 1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p (50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have little or no effect on the oxygen affinity. These effects are primarily associated with the binding of —SH groups, and are largely reversed on the addition of glutathione. —SH groups do not appear to be responsible for the Bohr effect. 2. Evidence is presented for the belief that the two hemes of each half-molecule of horse hemoglobin are situated on either side of a cluster of—SH groups. 3. The mechanism of interaction between the hemes is discussed. It is concluded that the reorganization of the protein architecture which accompanies oxygenation plays a central role in this interaction, in agreement with the views of Pauling and Wyman. |
format | Text |
id | pubmed-2147547 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1956 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21475472008-04-23 SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN Riggs, Austen F. Wolbach, Robert A. J Gen Physiol Article 1. Addition of 2 moles of mersalyl, mercuric chloride, p-chloromercuribenzoate (PCMB), or methyl mercury hydroxide per mole of hemoglobin greatly reduces heme-heme interactions (n), yet these substances have quite different effects on the oxygen affinity (-log p (50)). Mersalyl and mercuric chloride at this concentration each increase the oxygen affinity, while PCMB and methyl mercury have little or no effect on the oxygen affinity. These effects are primarily associated with the binding of —SH groups, and are largely reversed on the addition of glutathione. —SH groups do not appear to be responsible for the Bohr effect. 2. Evidence is presented for the belief that the two hemes of each half-molecule of horse hemoglobin are situated on either side of a cluster of—SH groups. 3. The mechanism of interaction between the hemes is discussed. It is concluded that the reorganization of the protein architecture which accompanies oxygenation plays a central role in this interaction, in agreement with the views of Pauling and Wyman. The Rockefeller University Press 1956-03-20 /pmc/articles/PMC2147547/ /pubmed/13295556 Text en Copyright © Copyright, 1956, 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 Riggs, Austen F. Wolbach, Robert A. SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title | SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title_full | SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title_fullStr | SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title_full_unstemmed | SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title_short | SULFHYDRYL GROUPS AND THE STRUCTURE OF HEMOGLOBIN |
title_sort | sulfhydryl groups and the structure of hemoglobin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2147547/ https://www.ncbi.nlm.nih.gov/pubmed/13295556 |
work_keys_str_mv | AT riggsaustenf sulfhydrylgroupsandthestructureofhemoglobin AT wolbachroberta sulfhydrylgroupsandthestructureofhemoglobin |