N-ethylmaleimide-modified heavy meromyosin. A probe for actomyosin interactions.
Keyword(s):
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.
1993 ◽
Vol 1153
(2)
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pp. 184-190
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Keyword(s):
1960 ◽
Vol 235
(10)
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pp. 2797-2800
1984 ◽
Vol 259
(7)
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pp. 4027-4030
1989 ◽
Vol 993
(1)
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pp. 21-26
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Inhibition by Palmitoyl CoA of EDTA- and Mg2+-ATPase of Heavy Meromyosin from Rabbit Skeletal Muscle
1981 ◽
Vol 90
(3)
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pp. 757-763
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2010 ◽
Vol 59
(4)
◽
pp. 337-348
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Keyword(s):
1995 ◽
Vol 73
(8)
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pp. 1154-1164
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1983 ◽
Vol 96
(6)
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pp. 1761-1765
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