N-Ethylmaleimide-Modified Heavy Meromyosin: A Probe for Actomyosin Interactions

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...

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Bibliographic Details
Published in:The Journal of cell biology 1979-07, Vol.82 (1), p.57-65
Main Authors: Meeusen, Ronald L., Cande, W. Zacheus
Format: Article
Language:English
Subjects:
Actins
Actins - metabolism
Actomyosin - metabolism
Adenosine triphosphatases
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Amoeba - drug effects
Amoeba - physiology
Animals
Calcium
Cell motility
Cells
Cytoplasm
Ethylmaleimide - pharmacology
Microfilaments
Microtubules
Myofibrils
Myofibrils - physiology
Myofibrils - ultrastructure
Myosin Subfragments - metabolism
Myosin Subfragments - pharmacology
Polymerization
Protein Binding
Rabbits
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.82.1.57