Correlation between multiple phosphorylation of gizzard myosin light chains and actin-activated myosin ATPase activity

With large amounts of gizzard Mr 135,000 calmodulin-binding protein (myosin light chain kinase), the phosphate incorporation into myosin light chains was determined to be 2 mol/mol of myosin light chain. The actin-activated ATPase activity was dramatically enhanced when myosin light chains were phos...

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Bibliographic Details
Published in:	Journal of biochemistry (Tokyo) Vol. 97; no. 6; p. 1823
Main Authors:	Tanaka, T, Yamazaki, K, Sobue, K
Format:	Journal Article
Language:	English
Published:	England 01-01-1985
Subjects:	Actins - physiology Adenosine Triphosphatases - metabolism Animals Chickens Enzyme Activation Gizzard, Avian - metabolism Myosin-Light-Chain Kinase Phosphorylation Protein Kinases - metabolism
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Summary:	With large amounts of gizzard Mr 135,000 calmodulin-binding protein (myosin light chain kinase), the phosphate incorporation into myosin light chains was determined to be 2 mol/mol of myosin light chain. The actin-activated ATPase activity was dramatically enhanced when myosin light chains were phosphorylated by more than 1 mol of phosphate incorporated/mol of myosin light chain.
ISSN:	0021-924X
DOI:	10.1093/oxfordjournals.jbchem.a135244