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STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN

1. Methods for the preparation and partial purification of streptococcal fibrinolysin are described. 2. The lysis of fibrin clots in the presence of streptococcal fibrinolysin is associated with proteolysis of the fibrin. Digestion is due to an enzyme normally present in serum or plasma in an inacti...

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Detalles Bibliográficos
Autor principal: Christensen, L. R.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1945
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142678/
https://www.ncbi.nlm.nih.gov/pubmed/19873427
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author Christensen, L. R.
author_facet Christensen, L. R.
author_sort Christensen, L. R.
collection PubMed
description 1. Methods for the preparation and partial purification of streptococcal fibrinolysin are described. 2. The lysis of fibrin clots in the presence of streptococcal fibrinolysin is associated with proteolysis of the fibrin. Digestion is due to an enzyme normally present in serum or plasma in an inactive state, which is activated by fibrinolysin. Fibrinolysin alone has no demonstrable proteolytic activity. 3. The lysin factor-fibrinolysin system brings about proteolysis of other proteins such as gelatin or casein, in addition to fibrin and fibrinogen. 4. It is suggested that lysin factor exists in serum or plasma as a zymogen, and that it is activated by fibrinolysin, a kinase, in a manner similar to the activation of trypsinogen by enterokinase or the mold kinase of Kunitz (1938).
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spelling pubmed-21426782008-04-23 STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN Christensen, L. R. J Gen Physiol Article 1. Methods for the preparation and partial purification of streptococcal fibrinolysin are described. 2. The lysis of fibrin clots in the presence of streptococcal fibrinolysin is associated with proteolysis of the fibrin. Digestion is due to an enzyme normally present in serum or plasma in an inactive state, which is activated by fibrinolysin. Fibrinolysin alone has no demonstrable proteolytic activity. 3. The lysin factor-fibrinolysin system brings about proteolysis of other proteins such as gelatin or casein, in addition to fibrin and fibrinogen. 4. It is suggested that lysin factor exists in serum or plasma as a zymogen, and that it is activated by fibrinolysin, a kinase, in a manner similar to the activation of trypsinogen by enterokinase or the mold kinase of Kunitz (1938). The Rockefeller University Press 1945-03-20 /pmc/articles/PMC2142678/ /pubmed/19873427 Text en Copyright © Copyright, 1945, 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
Christensen, L. R.
STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title_full STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title_fullStr STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title_full_unstemmed STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title_short STREPTOCOCCAL FIBRINOLYSIS: A PROTEOLYTIC REACTION DUE TO A SERUM ENZYME ACTIVATED BY STREPTOCOCCAL FIBRINOLYSIN
title_sort streptococcal fibrinolysis: a proteolytic reaction due to a serum enzyme activated by streptococcal fibrinolysin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142678/
https://www.ncbi.nlm.nih.gov/pubmed/19873427
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