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- W2023135466 abstract "The major active protein phosphatase present in a rabbit skeletal muscle extract is associated with the glycogen particle and migrates in sucrose density gradient centrifugation as a Mr = 70,000 protein and contains modulator activity. Addition of extra modulator protein causes a time- and concentration-dependent conversion of the enzyme to an inactive FA-ATP, Mg-dependent form. The intrinsic modulator in the active phosphatase is destroyed by limited proteolysis without an appreciable change in the phosphatase activity. The proteolyzed active enzyme has a lower molecular weight (Mr=40,000) and it reassociates with the modulator producing a FA-ATP, Mg-dependent enzyme form (Mr=60,000). The modulator protein is used stoichiometrically in the activation of the ATP, Mg-dependent phosphatase. This is in agreement with the presence of one unit of modulator activity per unit of native spontaneously active phosphatase." @default.
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- W2023135466 date "1983-09-01" @default.
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- W2023135466 title "Role of the modulator protein in the interconversion of rabbit skeletal muscle protein phosphatase" @default.
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- W2023135466 doi "https://doi.org/10.1016/s0006-291x(83)80015-1" @default.
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