Colchicine-binding Protein from Human Platelets and Its Effect on Muscle Myosin and Platelet Myosin-like Thrombosthenin-M

From the ¹ From the Department of Hematology, Mount Sinai School of Medicine, New York, New York 10029, and the Department of Neurology, Columbia University, College of Physicians and Surgeons, New York, New York 10032

A colchicine-binding protein was isolated from sonically treated platelets by ammonium sulfate precipitation (40 to 50% saturation), followed by elution from DEAE-Sephadex A-50 with a KCl gradient. Disc electrophoresis revealed one major protein band. This protein bound 0.042 µmole of colchicine per 100 mg; it lacked ATPase activity, but markedly altered the cation requirements for the ATPase activity of both muscle myosin and thrombosthenin-M, and when added to either muscle myosin or thrombosthenin-M, produced a rise in relative viscosity which fell sharply upon addition of ATP.

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