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Role of calmodulin (delta-subunit) in activation of phosphorylase kinase from rabbit skeletal muscles

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5727150

The structure of the inactivated and activated forms of phospholyase kinase was compared. The enzyme was activated by incubation in an alkaline medium (pH 8.5), phosphorylation of the catalytic subunit of cAMP-dependent protein kinase, and limited proteolysis. Hydrophobic chromatography on phenyl-Sepharose and electrophoresis in a polyacrylamide gel density gradient were employed for a comparison of these forms of the enzyme. Activation of the enzyme was accompanied by the separation of a low-molecular-weight component (M/sub r/ about 17,000). The low-molecular-weight protein was obtained in a homogeneous state by chromatography on phenyl-Sepharose. It was established that its properties are similar to those of calmodulin. The presence of calmodulin in preparations of phosphorylase kinase was judged by the activation of the calmodulin-dependent form of phosphodiesterase. The boiled and subtilisin-treated kinase activates phosphodiesterase in much the same way as bovine brain calmodulin. The results obtained suggest that the delta-subunit is a protein inhibitor of the enzyme.

Research Organization:
M.V. Lomonosov Moscow State Univ., USSR
OSTI ID:
5727150
Journal Information:
Biochemistry (Engl. Transl.); (United States), Journal Name: Biochemistry (Engl. Transl.); (United States) Vol. 51:4; ISSN BIORA
Country of Publication:
United States
Language:
English