Adelstein R S, Pollard T D, Kuehl W M
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2703-7. doi: 10.1073/pnas.68.11.2703.
Platelet myosin (thrombosthenin M) and two additional proteins corresponding to the head and rod portion of the myosin molecule have been prepared from human blood platelets. Characterization of these proteins by SDS-polyacrylamide gel electrophoresis, actin binding studies, assay of enzymic ATPase activity, and electron microscopy has shown that the platelet contractile proteins closely resemble the corresponding muscle proteins. Platelet myosin and platelet myosin-head bind to both muscle and platelet actin and have an EDTA + K-stimulated ATPase activity, which is suppressed by Mg(2+) in high salt concentration, whereas platelet rod does not possess either of these properties; platelet myosin and platelet myosin rod aggregate to form thick filaments at low ionic strength. Both intact platelet myosin and myosin head form typical arrowhead-shaped complexes with either platelet or muscle F-actin.
已从人血血小板中制备出血小板肌球蛋白（血栓收缩蛋白M）以及另外两种分别对应于肌球蛋白分子头部和杆部的蛋白质。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、肌动蛋白结合研究、酶促ATP酶活性测定和电子显微镜对这些蛋白质进行表征，结果表明血小板收缩蛋白与相应的肌肉蛋白极为相似。血小板肌球蛋白和血小板肌球蛋白头部可与肌肉和血小板肌动蛋白结合，并具有EDTA + K刺激的ATP酶活性，在高盐浓度下该活性会被Mg(2+)抑制，而血小板杆部不具备这两种特性；血小板肌球蛋白和血小板肌球蛋白杆部在低离子强度下会聚集形成粗丝。完整的血小板肌球蛋白和肌球蛋白头部与血小板或肌肉F-肌动蛋白均形成典型的箭头状复合物。
