Jan 1, 1975

The identification and subcellular localization of thrombosthenin "M", the myosin-like component of pig platelets

Journal of Mechanochemistry & Cell Motility
G L Harris, N Crawford


A protein has been studied which spontaneously precipitates from stored fractions of platelet soluble phase prepared by density gradient centrifugation. It is rich in a Ca2+ ATPase activity which displays an activity/pH profile resembling that of skeletal muscle myosin. Adjustment of freshly prepared soluble phase fractions to 0.6 M with respect to KCl and dilution 1 in 3 results in the precipitations of a protein fraction with essentially the same enzymatic properties as the spontaneously precipitable protein. These two similar proteins represent between 9 and 13% of the soluble phase total protein and each account for almost the whole of divalent cation activated ATPase activity of the soluble phases from which they were derived. The Mg2+ ATPase activity is only about twice purified with respect to the soluble phase enzyme activity, but the Ca2+ ATPase shows a 10-13-fold enrichment. Synthetic actomyosins can be prepared from the two proteins by addition of either platelet or skeletal muscle actin. These show significant increases in Mg2+ ATPase at the most favourable combination ratios. The ratio between the yield of soluble phase protein obtained by dilution precipitation and the lactate dehydrogenase activity of the soluble...Continue Reading

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Mentioned in this Paper

Establishment and Maintenance of Localization
Centrifugation, Density Gradient
Cations, Divalent
Ca(2+)-Transporting ATPase
Serum Proteins
Staphylococcal Protein A

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