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Phosphorylation of Nonmuscle Myosin by Calcium-Dependent and Independent Protein Kinases

Nonmuscle myosin from bovine thymus was purified, characterized , and phosphorylated with MLCK, H4PK, and Protein Kinase C. Phosphorylation occured exclusively on the myosin regulatory light chain. Phosphorylation by MLCK and H4PK resulted in the activation of the MgATPase activity as well as filament assembly of nonmuscle myosin.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc798346
Date12 1900
CreatorsHassell, Tommy C. (Tommy Clarence)
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
FormatText
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights

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