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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
› Author Affiliations
Further Information

Publication History

Received 24 April 1984

Accepted 21 July 1984

Publication Date:
19 July 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.

Keywords

Tissue thromboplastin - Concanavalin A - Glycosylation - Affinity chromatography
 

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