BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR

Decrease in the protease activity of the culture fluid observed at later stages of the antigen-antibody reaction is believed to be due to the release of an inhibitor by the cells. The inhibitor was submitted to partial purification: it is heat-stable, non-precipitated by trichloracetic acid and non-...

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Detalles Bibliográficos
Autores principales: Tokuda, Akira, Hayashi, Hideo, Matsuba, Kinishiro
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1960
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137229/
https://www.ncbi.nlm.nih.gov/pubmed/13777225
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author Tokuda, Akira
Hayashi, Hideo
Matsuba, Kinishiro
author_facet Tokuda, Akira
Hayashi, Hideo
Matsuba, Kinishiro
author_sort Tokuda, Akira
collection PubMed
description Decrease in the protease activity of the culture fluid observed at later stages of the antigen-antibody reaction is believed to be due to the release of an inhibitor by the cells. The inhibitor was submitted to partial purification: it is heat-stable, non-precipitated by trichloracetic acid and non-dialyzable. It inhibits certain cellular and tissue proteases and papain but is inactive against trypsin. It is suggested that the balance between protease and anti-protease released may determine the intensity, extent, and duration of certain sensitization phenomena.
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spelling pubmed-21372292008-04-17 BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR Tokuda, Akira Hayashi, Hideo Matsuba, Kinishiro J Exp Med Article Decrease in the protease activity of the culture fluid observed at later stages of the antigen-antibody reaction is believed to be due to the release of an inhibitor by the cells. The inhibitor was submitted to partial purification: it is heat-stable, non-precipitated by trichloracetic acid and non-dialyzable. It inhibits certain cellular and tissue proteases and papain but is inactive against trypsin. It is suggested that the balance between protease and anti-protease released may determine the intensity, extent, and duration of certain sensitization phenomena. The Rockefeller University Press 1960-08-01 /pmc/articles/PMC2137229/ /pubmed/13777225 Text en Copyright © Copyright, 1960, 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
Tokuda, Akira
Hayashi, Hideo
Matsuba, Kinishiro
BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title_full BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title_fullStr BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title_full_unstemmed BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title_short BIOCHEMICAL STUDY OF CELLULAR ANTIGEN-ANTIBODY REACTION IN TISSUE CULTURE : II. RELEASE OF A PROTEASE INHIBITOR
title_sort biochemical study of cellular antigen-antibody reaction in tissue culture : ii. release of a protease inhibitor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2137229/
https://www.ncbi.nlm.nih.gov/pubmed/13777225
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AT matsubakinishiro biochemicalstudyofcellularantigenantibodyreactionintissuecultureiireleaseofaproteaseinhibitor

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