THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.

1. The unsaturated lipoids (serum antitrypsin) can be adsorbed from guinea pig serum, rabbit serum, and horse serum by kaolin, starch, agar, and bacteria. 2. Diphtheria toxin and cobra venom also reduce the serum antitrypsin, possibly because of their affinity for lipoids. 3. Anaphylatoxins represen...

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Detalles Bibliográficos
Autores principales: Jobling, James W., Petersen, William
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1914
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2125178/
https://www.ncbi.nlm.nih.gov/pubmed/19867801
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author Jobling, James W.
Petersen, William
author_facet Jobling, James W.
Petersen, William
author_sort Jobling, James W.
collection PubMed
description 1. The unsaturated lipoids (serum antitrypsin) can be adsorbed from guinea pig serum, rabbit serum, and horse serum by kaolin, starch, agar, and bacteria. 2. Diphtheria toxin and cobra venom also reduce the serum antitrypsin, possibly because of their affinity for lipoids. 3. Anaphylatoxins represent sera rendered toxic by partial removal of serum antitrypsin. 4. The matrix of the protein split products lies in the serum proteins so exposed. 5. The amount of removal of serum antitrypsin depends on definite quantitative relations; very large amounts and very small amounts of adsorbing substances are least effective (kaolin, starch, and bacteria). 6. Bacteria previously treated with serum or with oils do not adsorb serum antitrypsin. 7. Bacteria treated with serum become more resistant to the action of trypsin.
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spelling pubmed-21251782008-04-18 THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV. Jobling, James W. Petersen, William J Exp Med Article 1. The unsaturated lipoids (serum antitrypsin) can be adsorbed from guinea pig serum, rabbit serum, and horse serum by kaolin, starch, agar, and bacteria. 2. Diphtheria toxin and cobra venom also reduce the serum antitrypsin, possibly because of their affinity for lipoids. 3. Anaphylatoxins represent sera rendered toxic by partial removal of serum antitrypsin. 4. The matrix of the protein split products lies in the serum proteins so exposed. 5. The amount of removal of serum antitrypsin depends on definite quantitative relations; very large amounts and very small amounts of adsorbing substances are least effective (kaolin, starch, and bacteria). 6. Bacteria previously treated with serum or with oils do not adsorb serum antitrypsin. 7. Bacteria treated with serum become more resistant to the action of trypsin. The Rockefeller University Press 1914-07-01 /pmc/articles/PMC2125178/ /pubmed/19867801 Text en Copyright © Copyright, 1914, 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
Jobling, James W.
Petersen, William
THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title_full THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title_fullStr THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title_full_unstemmed THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title_short THE MECHANISM OF ANAPHYLATOXIN FORMATION : STUDIES ON FERMENT ACTION. XV.
title_sort mechanism of anaphylatoxin formation : studies on ferment action. xv.
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2125178/
https://www.ncbi.nlm.nih.gov/pubmed/19867801
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