Daniel J L, Holmsen H, Adelstein R S
Thromb Haemost. 1977 Dec 15;38(4):984-9.
A 20,000 dalton polypeptide, which is phosphorylated in intact platelets pre-incubated with 32P-PO4, has been identified as a platelet myosin light chain. Stimulation of intact platelets with thrombin produced a 5-fold increase in the amount of radioactive phosphate incorporated into the light chain. Myosin phosphorylation preceeded acid hydrolase secretion and occurred concomitantly with adenine nucleotide secretion. These results are suggestive of participation of contractile mechanisms in platelet secretion.
一种20000道尔顿的多肽，在与32P-PO4预孵育的完整血小板中发生磷酸化，已被鉴定为血小板肌球蛋白轻链。用凝血酶刺激完整血小板，会使掺入轻链中的放射性磷酸盐量增加5倍。肌球蛋白磷酸化先于酸性水解酶分泌，并与腺嘌呤核苷酸分泌同时发生。这些结果提示收缩机制参与了血小板分泌。
