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Identification of casein kinase II as a major endogeneous caldesmon kinase in sheep aorta smooth muscle
Author(s) -
Vorotniko Alexander V.,
Gusev Nikolai B.,
Hua Suming,
Collins John H.,
Redwood Charles S.,
Marston Steven B.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81671-l
Subject(s) - caldesmon , casein kinase 2 , casein kinase 2, alpha 1 , myosin , biochemistry , microbiology and biotechnology , myofibril , phosphorylation , kinase , chemistry , protein kinase a , calmodulin , casein kinase 1 , biology , enzyme , mitogen activated protein kinase kinase
A caldesmon kinase activity was detected in an ATP extract of the myofibril‐like pellet from sheep aorta. The enzyme was purified 745‐fold and was identified as casein kinase II on the basis of molecular size, substrate specificity, and high sensitivity to heparin inhibition. Casein kinase II phosphorylated isolated caldesmon and caldesmon incorporated into native thin filaments, and transferred about 1 mol of phosphate per mol of caldesmon‐ h . Ser‐73 was the main site phosphorylated by casein kinase II in chicken gizzard caldesmon. Phosphorylation of caldesmon reduced its affinity for smooth muscle myosin but had no effect upon the ability of caldesmon to inhibit the ATPase activity of actomyosin.