Inhibition by Palmitoyl CoA of EDTA- and Mg2+-ATPase of Heavy Meromyosin from Rabbit Skeletal Muscle

1981 ◽  
Vol 90 (3) ◽  
pp. 757-763 ◽  
Author(s):  
Akiko FUJIWARA ◽  
Hisao FUJISAKI ◽  
Hiroshi ASAI ◽  
Ikuo YASUMASU
1979 ◽  
Vol 82 (1) ◽  
pp. 57-65 ◽  
Author(s):  
R L Meeusen ◽  
W Z Cande

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.


1960 ◽  
Vol 235 (10) ◽  
pp. 2797-2800
Author(s):  
Patricia Z. Thomas ◽  
Enrico Forchielli ◽  
Ralph I. Dorfman

1993 ◽  
Vol 268 (20) ◽  
pp. 14687-14693 ◽  
Author(s):  
Y. Cao ◽  
A.M. Mahrenholz ◽  
A.A. DePaoli-Roach ◽  
P.J. Roach

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