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  • Title: N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.
    Author: Meeusen RL, Cande WZ.
    Journal: J Cell Biol; 1979 Jul; 82(1):57-65. PubMed ID: 158029.
    Abstract:
    Treatment of rabbit skeletal muscle heavy meromyosin (HMM) with the sulfhydryl reagent N-ethylmaleimide (NEM) produces a species of HMM which remains tightly bound to actin in the presence of MgATP. NEM-HMM forms characteristic "arrowhead" complexes with actin which persist despite rinses with MgATP. NEM-HMM inhibits the actin activation of native HMM-ATPase activity, the superprecipitation of actomyosin, the contraction of glycerinated muscle myofibrils, and the contraction of cytoplasmic strands of the soil amoeba Chaos carolinensis. However, NEM-HMM does not interfere with in vitro microtubule polymerization or beating of demembranated cilia.
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