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  • Title: The role of actin sulfhydryls in actin-myosin interaction.
    Author: Heazlitt R, Conway G, Montag J.
    Journal: Biochim Biophys Acta; 1973 Aug 30; 317(2):316-27. PubMed ID: 19999717.
    Abstract:
    Rabbit white skeletal and dog cardiac actins combined fully with the heavy meromyosins at 4 degrees C and low ionic strength (10.03); the complexes (actin-heavy meromyosin) were mostly in a heavy component which settled rapidly during rotor acceleration. Increasing the temperature to 24 degrees C favored formation of the heavy component while increasing the ionic strength to 10.3 decreased formation of the heavy component. Modification of actin with p-mercuribenzoate (PCMB) generally reduced the heavy component and viscosity but did not interfere with actin-heavy meromyosin combination. Modification with iodoacetamide or N-ethylmaleimide had similar effects. Addition of ATP reduced viscosity and eliminated the heavy component at levels which partially dissociated actin-heavy meromyosin. Modification of heavy meromyosin with PCMB inhibited combination with actin. The characteristics of interaction of the cardiac proteins varied less with temperature but more with ionic strength than those of skeletal proteins.
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