Platelet myosin. Localization of the rod myosin fragment and effect of its antibodies on platelet function.

Abstract

Partial hydrolysisof human platelet or uterine smooth muscle myosin with insoluble papain yielded rod fragments, insoluble at low ionic strength and devoid of ATPase activity.This protein migrated on sodium dodecyl sulfate-8 M urea gel electrophoresis as a single band with a molecular weight of approximately 110,000 to 120,000 corresponding to the rod portion of myosin.Rabbit antibodies to platelet and uterine rod myosin were highly specific by the criteria of double-gel diffusion and immunoelectrophoresis; they reacted with a single precipitin line against actomyosin and rod myosin from their respective tissue sources, but failed to cross-react.Antibodies to platelet rod myosin inhibited superprecipitation of platelet actomyosin but did not inhibit its ATPase activity.The surface of blood platelets was stained by an indirect immunofluorescence technique with antiserum to human platelet rod myosin but not with antiserum to uterine rod myosin. Fluorescencewas never intense,