Add time:09/02/2019         Source:sciencedirect.com

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).We have been studying the mechanism of ristocetin-induced platelet aggregation in an attempt to establish the relationship between the antibiotic-induced platelet aggregation and the platelet adhesion of primary thrombosis. To facilitate these studies, we investigated the use of ristocetin which was labeled with 125I. We have developed a mild technique for iodinating ristocetin such that it retains its platelet aggregating activity and exhibits physical and chemical properties similar to those of unlabeled ristocetin.

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