Abstract
THE surface of the human blood platelet is rich in carbohydrate and at least four glycoprotein components have been resolved by gel electrophoresis of isolated platelet plasma membranes1. Two platelet disease states are characterised by a diminution or absence of certain of these glycoproteins2–5: in the case of Bernard-Soulier disease, glycoprotein I (molecular weight (MW) 150,000) is lacking while platelet membranes isolated from patients suffering from Glanzmann's thrombasthenia lack glycoprotein II (MW 120,000). While screening several patients with ill-defined but clinically evident haemostatic problems, we have now identified two unrelated individuals who show an abnormal polymorphic pattern of glycoprotein distribution within their platelet membranes and a concomitant reduction in the ability of the intact platelets to bind thrombin.
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BOLIN, R., OKUMURA, T. & JAMIESON, G. New polymorphism of platelet membrane glycoproteins. Nature 269, 69–70 (1977). https://doi.org/10.1038/269069a0
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DOI: https://doi.org/10.1038/269069a0
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