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A cofactor protein required for actin activation of myosin Mg2+ATPase activity in leukemic myeloblasts.

Authors
Type
Published Article
Journal
Journal of biochemistry
Publication Date
Volume
92
Issue
6
Pages
1845–1851
Identifiers
PMID: 6131068
Source
Medline
License
Unknown

Abstract

The Mg2+ATPase activity of the myosin of a myeloid leukemia cell line (Ml) was not activated by purified Ml actin or by muscle actin alone. Activation required the presence of a cellular fraction as a cofactor in addition to the actin, when Mg2+ATPase was stimulated as much as 20-fold. The cofactor was partially purified and characterized. 1) Its molecular weight was estimated as 45,000 to 55,000 daltons by gel filtration and as 45,000 daltons by SDS polyacrylamide gel electrophoresis. 2) The cofactor was a light chain kinase that phosphorylated both the L1 and L2 light chains of the Ml cell myosin, but not the L3 or heavy chain.

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