ATP hydrolysis and sliding movement of actomyosin complex in the presence of ethanol.
We measured both the ATPase activity of actomyosin complex and the sliding velocity of actin filaments on myosin heads under hydrophobic conditions in the presence of ethanol. Both the ATPase activity and the sliding velocity decrease with the increase of ethanol concentration, if the ionic strength is not too high. As ionic strength increases, there appears an optimum concentration of ethanol that can enhance both the ATPase activity and the sliding velocity.
Hatori
K
K
Department of BioEngineering, Nagaoka University of Technology, Niigata.
Honda
H
H
Matsuno
K
K
D000205:Actomyosin / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D000431:Ethanol / Q000494:pharmacology*; D007700:Kinetics; D018482:Muscle, Skeletal / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits
D000431:Ethanol; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins