Human Platelet Myosin
Year: 1971
Type: article
Abstract: A rapid purification procedure for myosin from human blood platelets is described. The isolated protein was found to be homogeneous by ultracentrifugation, free diffusion, and immunochemical criteria. The following physical parameters of the protein were established; sedimentation coefficient (s20, w0) 6.8 S; diffusion coefficient (D20, w) (from boundary spreading during free diffusion), 1.13 x 10-7 cm2 sec-1; partial specific volume (v), 0.731 ml g-1; molecular weight, 542,700 g mole-1; and frictional ratio (f/f0), 3.48. The amino acid composition of platelet myosin is reported. Divalent cations such as Ca++ and Mg++ activated the myosin ATPase activity, whereas EDTA inhibited the enzyme activity. Succinylation of platelet myosin indicated the presence of a large subunit with sedimentation coefficient (s20, w0) of 4.9 S. In addition, electron micrographs of two types of negatively stained (uranyl acetate) polymerized platelet myosin (types I and III) are shown.
Source: Journal of Biological Chemistry
Institution: Rush University Medical Center
Language: French
Subfield: Cardiology and Cardiovascular Medicine
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1987845244