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LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME

Antibodies to crystalline bovine hepatic L-glutamic dehydrogenase were induced in rabbits. These antibodies inhibited the bovine glutamic dehydrogenase used as antigen, and also inhibited glutamic dehydrogenases from rat, rabbit, human, pigeon, and frog livers, as well as frog renal and muscle gluta...

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Detalles Bibliográficos
Autores principales: Bollet, Alfred Jay, Davis, John S., Hurt, John O.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1962
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137407/
https://www.ncbi.nlm.nih.gov/pubmed/13870814
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author Bollet, Alfred Jay
Davis, John S.
Hurt, John O.
author_facet Bollet, Alfred Jay
Davis, John S.
Hurt, John O.
author_sort Bollet, Alfred Jay
collection PubMed
description Antibodies to crystalline bovine hepatic L-glutamic dehydrogenase were induced in rabbits. These antibodies inhibited the bovine glutamic dehydrogenase used as antigen, and also inhibited glutamic dehydrogenases from rat, rabbit, human, pigeon, and frog livers, as well as frog renal and muscle glutamic dehydrogenase. The antibody did not inhibit yeast glutamic dehydrogenase which differs from the animal enzymes in cofactor requirement. The kinetic characteristics of the inhibition of the bovine glutamic dehydrogenase indicate mixed competitive and non-competitive inhibition, suggesting reaction with multiple antigenic sites; the data indicate competitive inhibition of the enzyme from other species, suggesting reaction with the catalytic site.
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spelling pubmed-21374072008-04-17 LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME Bollet, Alfred Jay Davis, John S. Hurt, John O. J Exp Med Article Antibodies to crystalline bovine hepatic L-glutamic dehydrogenase were induced in rabbits. These antibodies inhibited the bovine glutamic dehydrogenase used as antigen, and also inhibited glutamic dehydrogenases from rat, rabbit, human, pigeon, and frog livers, as well as frog renal and muscle glutamic dehydrogenase. The antibody did not inhibit yeast glutamic dehydrogenase which differs from the animal enzymes in cofactor requirement. The kinetic characteristics of the inhibition of the bovine glutamic dehydrogenase indicate mixed competitive and non-competitive inhibition, suggesting reaction with multiple antigenic sites; the data indicate competitive inhibition of the enzyme from other species, suggesting reaction with the catalytic site. The Rockefeller University Press 1962-07-01 /pmc/articles/PMC2137407/ /pubmed/13870814 Text en Copyright © Copyright, 1962, by The Rockefeller Institute 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
Bollet, Alfred Jay
Davis, John S.
Hurt, John O.
LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title_full LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title_fullStr LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title_full_unstemmed LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title_short LACK OF SPECIES SPECIFICITY OF ANTIBODY TO AN ENZYME
title_sort lack of species specificity of antibody to an enzyme
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137407/
https://www.ncbi.nlm.nih.gov/pubmed/13870814
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