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PMID: 158029 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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

The Journal of cell biology ·Vol. 82 ·No. 1 ·1979-07-00 ·Pages 57-65

Meeusen RL, Cande WZ

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.

MeSH Terms
Actins/metabolism Actomyosin/metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Amoeba/drug effects,physiology Animals Ethylmaleimide/pharmacology Myofibrils/physiology,ultrastructure Myosin Subfragments/metabolism,pharmacology Protein Binding Rabbits
Chemicals
Actins Myosin Subfragments Adenosine Triphosphate Actomyosin Adenosine Triphosphatases Ethylmaleimide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Meeusen R L
Cande W Z
References (35)
35 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.82.1.57
Published
1979-07-00
Pages
57-65
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2110416
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.82.1.57 PMC Full Text View journal details
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