Literature DB >> 210494

Comparison of the reactions of neutral granulocyte proteases with the major plasma protease inhibitors and with antiplasmin.

K Ohlsson, D Collen.   

Abstract

Reaction mixtures of human serum and increasing amounts of granulocyte collagenase, elastase and chymotrypsin-like enzyme were studied by crossed immunoelectrophoresis utilizing antibodies against alpha1-antitrypsin, alpha1-antichymotrypsin, and antiplasmin. The increasing complex formation of alpha1-antitrypsin and alpha 1-antichymotrypsin with the different granulocyte proteases was not accompanied by any changes in the electrophoretic mobility or precipitate pattern of antiplasmin until the protease binding capacity of serum was saturated. The antiplasmin component in the reaction mixtures of human serum and granulocyte collagenase or elastase was not precipitated by antibodies against the proteases. The results indicate that none of the granulocyte proteases are bound by antiplasmin and that these enzymes do not activate plasminogen in serum.

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Year:  1977        PMID: 210494     DOI: 10.3109/00365517709092640

Source DB:  PubMed          Journal:  Scand J Clin Lab Invest        ISSN: 0036-5513            Impact factor:   1.713


  2 in total

Review 1.  Natural inhibitors of fibrinolysis.

Authors:  D Collen
Journal:  J Clin Pathol Suppl (R Coll Pathol)       Date:  1980

2.  Protease inhibitors in rheumatoid synovial fluid. Analyses of electrophoretic homogeneity and protease inhibitory capacity.

Authors:  L Ekerot; K Ohlsson
Journal:  Rheumatol Int       Date:  1982       Impact factor: 2.631

  2 in total

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