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Phosphorylation of chicken gizzard myosin and the Ca 2+ ‐sensitivity of the actin‐activated Mg 2+ ‐ATPase
Author(s) -
Cole Heather A.,
Patchell Valerie B.,
Perry S.Victory
Publication year - 1983
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(83)80667-x
Subject(s) - myosin , phosphorylation , gizzard , myosin light chain kinase , actin , atpase , chemistry , immunoglobulin light chain , biochemistry , biophysics , microbiology and biotechnology , biology , enzyme , paleontology , antibody , immunology
A method is described for the preparation of partially and fully phosphorylated chicken gizzard myosin. When fully phosphorylated it possessed an actin‐activated Mg 2+ ‐ATPase of similar specific activity to that of mammalian skeletal muscle myosin. The Mg 2+ ‐ATPase activity of these preparations was related in a non‐linear fashion to increasing phosphorylation of the P light chain. When P light chain phosphorylation occurred during enzymic assay the Mg 2+ ‐ATPase activity remained constant. Fully phosphorylated preparations of gizzard myosin possessed an actin‐activated Mg 2+ ‐ATPase that was not Ca 2+ ‐sensitive, whereas the Mg 2+ ‐ATPase of partially phosphorylated myosin preparations was Ca 2+ ‐sensitive.