scholarly journals The Reduction in Vitro of 17α-Hydroxypregnenolone (3β,17α-Dihydroxy-Δ5-pregnen-20-one) by Rabbit Skeletal Muscle

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

In vitro binding of dantrolene to sarcoplasmic reticulum of rabbit skeletal muscle

1982 ◽  
Vol 31 (6) ◽  
pp. 965-968 ◽  
Author(s):  
Ahmad Reza Dehpour ◽  
Siavoosh Mofakham ◽  
Massoud Mahmoudian
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Rabbit Skeletal Muscle ◽  
In Vitro Binding ◽  
Vitro Binding

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

1979 ◽  
Vol 82 (1) ◽  
pp. 57-65 ◽  
Author(s):  
R L Meeusen ◽  
W Z Cande
Keyword(s):  
Skeletal Muscle ◽  
Atpase Activity ◽  
Rabbit Skeletal Muscle ◽  
Heavy Meromyosin ◽  
Sulfhydryl Reagent ◽  
Microtubule Polymerization ◽  
Soil Amoeba ◽  
Glycerinated Muscle

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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