Preparation and platelet aggregating activity of I-labeled ristocetin |
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Authors: | Robert F. BaughJames E. Brown Cecil Hougie |
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Affiliation: | Department of Pathology, M-012, University of California, San Diego, La Jolla, California 92093 USA |
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Abstract: | The antibiotic ristocetin is a glycoproteoid isolated from the culture media of Nocardia lurida N.R.R.L. 2430 whose structural features have yet to be resolved (1–3). The antibiotic has been studied both for its antibiotic properties (4–6) and, more recently, for its inducement of platelet aggregation in humans, both in vivo and in vitro (7–9). This latter phenomena resulted in the discontinued use of ristocetin in antibiotic therapy (10), but has provided a useful tool for studying the bleeding disorder, von Willebrand's disease. The disease is genetic in origin and is characterized by the lack of a functional plasma protein believed to be required for the adhesion of platelets to vascular epithelia during primary thrombotic events (11). This plasma protein, termed von Willebrand's factor, is also necessary to support ristocetin-induced platelet aggregation of human platelets (12). Thus, ristocetin has found increasing use not only in facilitating the diagnosis of von Willebrand's disease but also in characterizing the plasma protein (13). |
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