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Thromb Haemost 1979; 42(02): 571-581
DOI: 10.1055/s-0038-1666895
Original Article
Schattauer GmbH Stuttgart

Action of Brinase on Human Fibrinogen and Plasminogen

Ph Vanhove
,
M B Donati
,
H Claeys
The Center for Thrombosis and Vascular Research, Medical Research Department, University of Leuven, Belgium
,
R Verhaeghe
The Center for Thrombosis and Vascular Research, Medical Research Department, University of Leuven, Belgium
,
J Vermylen
The Center for Thrombosis and Vascular Research, Medical Research Department, University of Leuven, Belgium
› Author Affiliations
Further Information

Publication History

Received 30 January 1978

Accepted 24 August 1978

Publication Date:
23 August 2018 (online)

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Summary

Brinase added to human plasma in vitro caused a decrease in fibrinogen concentration, positive paracoagulation tests and formation of a friable clot in sequence. Agarose gel filtration of these samples revealed the presence of fibrinogen derivatives both larger and smaller than the parent molecule. Infusion of the enzyme in vivo resulted in a decreased fibrinogen level, a prolonged thrombin time and an increase in fibrinogen related antigen (FRA) in serum. The elution pattern of FRA in the plasma samples obtained after infusion of Brinase was similar to that of the in vitro samples. The plasma pool of fibrinogen was partially consumed by infusion of Brinase, but the turnover of plasminogen remained unaffected. Purified plasminogen was partially degraded by addition of the enzyme but this was not accompanied by a generation of proteolytic activity. These findings confirm that Brinase induces a proteolytic degradation of fibrinogen in plasma without activation of the plasminogen-plasmin system. Exposure of polymerization site(s) in the fibrinogen molecule is probably responsible for the reported clot promoting effect of the enzyme.