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The interaction between pyrophosphate and Mg on superprecipitation and ATPase activity of actomyosin

, : The interaction between pyrophosphate and Mg on superprecipitation and ATPase activity of actomyosin. Sapporo Med Jour 11(2/3): 81-86

The behavior of adenosine triphosphatase (ATPase) and superprecipitation of actomyosin after treatment with inorganic pyrophosphate in a low KC1 concentration was studied. The effect of 10-2[image] pyrophosphate on myosin B-ATPase was removed by addition of 10-4[image] MgCl2. The isoelectric precipitation of myosin B was reversed by pyrophosphate, and then returned to its original state in the presence of Mg. In this condition, superprecipitation was likewise regenerated and each step in the process of the superprecipitation, namely the clear phase, aggregation and syneresis, became similar to the case without pyrophosphate or Mg. From these results, the importance of bivalent metal, especially Mg++, on the ATPase activity and deformation of myosin B was discussed.


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