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PubMed · 158029

N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.

R L Meeusen·W Z Cande
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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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ActinsActomyosinAdenosine TriphosphatasesAdenosine TriphosphateAmoebaAnimalsEthylmaleimideMyofibrilsMyosin SubfragmentsProtein BindingRabbitsJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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R L Meeusen, W Z Cande. 1979. N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.. https://doi.org/10.1083/jcb.82.1.57

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