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Thromb Haemost 1984; 52(02): 192-195
DOI: 10.1055/s-0038-1661170
DOI: 10.1055/s-0038-1661170
Original Article
Interaction of Thromboplastin Apoprotein of Different Tissues with Concanavalin A - Evidence for Heterogeneous Glycosylation of the Human Apoprotein
Further Information
Publication History
Received 24 April 1984
Accepted 21 July 1984
Publication Date:
19 July 2018 (online)


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.