Literature DB >> 137236

2,4-Dinitrophenol as a specific inhibitor of the breakdown of the actomyosin-phosphate-ADP complex.

Y Yamaka, A Inoue, S Watanabe.   

Abstract

2,4-Dinitrophenol (DNP) was found to cause a "clearing response" of myosin B in a medium in which "superprecipitation" of myosin B would otherwise take place. The effect of actin concentration on Mg-ATPase [EC 3.6.1.3] of HMM was studied in the presence and absence of DNP. The results indicate that DNP causes an increase rather than a decrease in the affinity of HMM for actin, and that it causes a decrease only in the actin-activated portion of the Mg-ATPase activity. Using a light-scattering technique, it was shown that neither the ATP-induced dissociation of acto-HMM nor subsequent reassociation is significantly affected by the presence of DNP. As for the formation of the myosin-phosphate-ADP complex in the myosin-ATPase reaction, it was shown that formation of the reactive complex is not affected by DNP. It can thus be concluded that DNP inhibits the decomposition of the actomyosin-phosphate-ADP complex, which is thought to be coupled with superprecipitation.

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Year:  1976        PMID: 137236     DOI: 10.1093/oxfordjournals.jbchem.a131367

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


  1 in total

1.  Specificity and kinetic effects of nitrophenol analogues that activate myosin subfragment 1.

Authors:  V P Salerno; A S Ribeiro; A N Dinucci; J A Mignaco; M M Sorenson
Journal:  Biochem J       Date:  1997-06-15       Impact factor: 3.857

  1 in total

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