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THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM

Antibodies to yeast d-glyceraldehyde 3-phosphate dehydrogenase have been produced in rabbits and chickens. The antiserum from either animal inhibits the activity of the yeast enzyme with the formation of a precipitate that has a low residual activity. One combining site of antibody on the enzyme app...

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Detalles Bibliográficos
Autores principales: Krebs, Edwin G., Najjar, Victor A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1948
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2135845/
https://www.ncbi.nlm.nih.gov/pubmed/18103396
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author Krebs, Edwin G.
Najjar, Victor A.
author_facet Krebs, Edwin G.
Najjar, Victor A.
author_sort Krebs, Edwin G.
collection PubMed
description Antibodies to yeast d-glyceraldehyde 3-phosphate dehydrogenase have been produced in rabbits and chickens. The antiserum from either animal inhibits the activity of the yeast enzyme with the formation of a precipitate that has a low residual activity. One combining site of antibody on the enzyme appears to be the point of DPN attachment. The rate of antigen-antibody formation has been studied with varying concentrations of antibody. The activity of yeast hexokinase is not inhibited by the antiserum to the dehydrogenase. Five of six antisera to the yeast enzyme showed no inhibition of the analogous enzyme from rabbit muscle, but one serum strongly inhibited the muscle dehydrogenase in the absence of DPN. No evidence was obtained that the inhibition by this one antiserum was due to an immune reaction, because the inhibition persisted after absorption with the homologous antigen.
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spelling pubmed-21358452008-04-18 THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM Krebs, Edwin G. Najjar, Victor A. J Exp Med Article Antibodies to yeast d-glyceraldehyde 3-phosphate dehydrogenase have been produced in rabbits and chickens. The antiserum from either animal inhibits the activity of the yeast enzyme with the formation of a precipitate that has a low residual activity. One combining site of antibody on the enzyme appears to be the point of DPN attachment. The rate of antigen-antibody formation has been studied with varying concentrations of antibody. The activity of yeast hexokinase is not inhibited by the antiserum to the dehydrogenase. Five of six antisera to the yeast enzyme showed no inhibition of the analogous enzyme from rabbit muscle, but one serum strongly inhibited the muscle dehydrogenase in the absence of DPN. No evidence was obtained that the inhibition by this one antiserum was due to an immune reaction, because the inhibition persisted after absorption with the homologous antigen. The Rockefeller University Press 1948-12-01 /pmc/articles/PMC2135845/ /pubmed/18103396 Text en Copyright © Copyright, 1948, by The Rockefeller Institute for Medical Research New York 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
Krebs, Edwin G.
Najjar, Victor A.
THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title_full THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title_fullStr THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title_full_unstemmed THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title_short THE INHIBITION OF d-GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE BY SPECIFIC ANTISERUM
title_sort inhibition of d-glyceraldehyde 3-phosphate dehydrogenase by specific antiserum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2135845/
https://www.ncbi.nlm.nih.gov/pubmed/18103396
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