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. 1973 Nov;70(11):3115–3119. doi: 10.1073/pnas.70.11.3115

Phosphorylation of Human Platelet Myosin

Robert S Adelstein 1, Mary Anne Conti 1, William Anderson Jr 1
PMCID: PMC427182  PMID: 4522294

Abstract

A preparation extracted from human blood platelets, which incorporates 32P from γ-labeled AT32P into one of the two light chains of platelet myosin and platelet myosin head is described. This phosphorylation, which appears to be due to an endogenous kinase, is specific for the myosin light chain in that no other protein extracted in 0.6 M KCl-15 mM Tris·HCl (pH 7.5) is phosphorylated. The phosphorylated light chain, which has been purified by gel filtration, releases the covalently bound phosphate after incubation in alkali and not after incubation in acid.

Keywords: myosin light chain, [γ-32P]ATP, contractile proteins, endogenous kinase

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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