Literature DB >> 7608109

ATP hydrolysis and sliding movement of actomyosin complex in the presence of ethanol.

K Hatori1, H Honda, K Matsuno.   

Abstract

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.

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Year:  1995        PMID： 7608109     DOI： 10.1093/jb/117.2.264

Source DB:  PubMed          Journal:  J Biochem        ISSN： 0021-924X            Impact factor:   3.387


  2 in total

1.  Dimethyl sulphoxide enhances the effects of P(i) in myofibrils and inhibits the activity of rabbit skeletal muscle contractile proteins.

Authors:  A C Mariano; G M Alexandre; L C Silva; A Romeiro; L C Cameron; Y Chen; P B Chase; M M Sorenson
Journal:  Biochem J       Date:  2001-09-15       Impact factor: 3.857

2.  Modulation of actomyosin motor function by 1-hexanol.

Authors:  Hideyuki Komatsu; Taeko Shigeoka; Tetsuo Ohno; Kuniyoshi Kaseda; Takeshi Kanno; Yoko Matsumoto; Makoto Suzuki; Takao Kodama
Journal:  J Muscle Res Cell Motil       Date:  2004       Impact factor: 2.698
  2 in total

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