Thromb Haemost 1981; 45(02): 154-157
DOI: 10.1055/s-0038-1650154
Original Article
Schattauer GmbH Stuttgart

Binding of 99mTc Plasminogen on Fibrin

I Juhan-Vague
1)   The Laboratoire d’Hématologie (Pr. R. Muratore), CHU Timone, Marseille, France
,
M F Calas
1)   The Laboratoire d’Hématologie (Pr. R. Muratore), CHU Timone, Marseille, France
,
F Roux
2)   Laboratoire d’Hématologie Isotopique (Pr. P. J. Bernard), CHU Timone, Marseille, France
,
C Juhan
3)   Service de Chirurgie Vasculaire (Pr. C. Juhan), Hôpital Nord, Marseille, France
,
F Durand-Dessemon
1)   The Laboratoire d’Hématologie (Pr. R. Muratore), CHU Timone, Marseille, France
,
C de Laforte
2)   Laboratoire d’Hématologie Isotopique (Pr. P. J. Bernard), CHU Timone, Marseille, France
,
A Serradimigni
4)   Service de Cardiologie (Pr. A. Serradimigni), CHU Timone, Marseille, France
› Author Affiliations
Further Information

Publication History

Received 28 November 1980

Accepted 22 January 1981

Publication Date:
05 July 2018 (online)

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Summary

Binding of plasminogen to fibrin was studied in vitro and in vivo using 99mTc Glu- and Lys-plasminogen.

Binding of Glu-plasminogen on the clot was not observed in vitro, and in vivo in the dog.

Conversely, the binding of Lys-plasminogen to fibrin displays a linear relationship to the concentration of Lys-plasminogen, up to doses exceeding equimolarity; thus suggesting the existence of several Lys-plasminogen binding sites on fibrin. Binding levels were identical, regardless of whether plasminogen was incubated in normal plasma or in plasma devoid of antiplasmin. In the dog, Lys-plasminogen bound specifically to the clot, however, clot sites could not be localized by scintigraphy in the dog or in man.