Platelet-binding of the von Willebrand factor

D. Green, H. P. Muller

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The aggregation of platelets by the antibiotic, ristocetin, requires a plasma cofactor (VIII:vWF) and one or more specific binding sites on the platelet membrane. The interaction between VIII:vWF and the platelet was examined using VIII:vWF labelled with 125I. In the presence of ristocetin (1.5 mg/ml), from 70 to 90% of the 125I-VIII:vWF became platelet-bound. By contrast, only 21% was bound with thrombin (2.5 U/ml), and 2.2% with buffer alone. Fractionation of the platelets revealed that peak radioactivity was present in the membrane fraction. Treatment of ristocetin-reacted platelets with either chymotrypsin, 100 μg/ml, or trypsin, 75 μg/ml, resulted in the partial release of the membrane-bound radioactivity. It is concluded that VIII:vWF binds to the platelet membrane in the presence of ristocetin.

Original languageEnglish (US)
Pages (from-to)689-694
Number of pages6
JournalThrombosis and Haemostasis
Volume39
Issue number3
DOIs
StatePublished - 1978

ASJC Scopus subject areas

  • Hematology

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