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  • Title: Isolation and characterization of two 70 kDa modulator-complexes from rabbit skeletal muscle.
    Author: Vandenheede JR, Vanden Abeele C, Merlevede W.
    Journal: Biochem Biophys Res Commun; 1986 Mar 13; 135(2):367-73. PubMed ID: 3008715.
    Abstract:
    The activation as well as the inactivation of the ATP,Mg-dependent protein phosphatase has been shown to be totally dependent upon the presence of the modulator subunit. This modulator (inhibitor-2) is a heat stable protein and its isolation in pure form (32 kDa) always includes a boiling step. The boiled modulator fractions are known to be inhibitory to the phosphatase activity. Unboiled rabbit skeletal muscle preparations do not contain "free modulator", but two higher molecular weight complexes (70 kDa) can be isolated which have the 32 kDa modulator together with a 38 kDa protein. One complex is the already characterized inactive ATP,Mg-dependent phosphatase [FCM] while the second one, [MX], although seemingly of identical composition, does not exhibit phosphatase activity when measured under the usual conditions. The MX-complex does not inhibit the phosphatase activity unless subjected to a boiling step which dissociates the modulator subunit. The unboiled [MX] exhibits the activation as well as the inactivation characteristics of the free modulator.
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