Thromb Haemost 1984; 52(02): 192-195
DOI: 10.1055/s-0038-1661170
Original Article
Schattauer GmbH Stuttgart

Interaction of Thromboplastin Apoprotein of Different Tissues with Concanavalin A - Evidence for Heterogeneous Glycosylation of the Human Apoprotein

A M H P van den Besselaar
Haemostasis and Thrombosis Research Unit, Leiden University Hospital, Leiden, The Netherlands
,
R M Bettina
Haemostasis and Thrombosis Research Unit, Leiden University Hospital, Leiden, The Netherlands
› Institutsangaben
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Publikationsverlauf

Received 24. April 1984

Accepted 21. Juli 1984

Publikationsdatum:
19. Juli 2018 (online)

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Summary

Thromboplastin apoproteins of different tissues were solubilized with Triton X-100. Induction of plasma coagulation by these extracts was dependent on the presence of factor VII. Binding of the apoprotein-Triton complex to Concanavalin A- Sepharose 4B was studied. The apoprotein activity extracted from rabbit brain and bovine brain was almost completely bound to Concanavalin A-Sepharose. Under the same conditions, only partial binding was observed with human lung, human brain and human placenta apoprotein. These results suggest that human apoprotein is heterogeneous with respect to its carbohydrate moiety.