PMID: 6108993Aug 1, 1980Paper

Ca2+- or Mg2+-dependent enzymatic ATP hydrolysis associated with the microsomal fraction of frog sciatic nerves

Journal of Neurochemistry
A EdströmM Wallin

Abstract

The microsomal fraction of frog sciatic nerves was found to contain Ca2+- or Mg2+-dependent hydrolytic activity toward different nucleoside di- and triphosphates. In the presence of Ca2+ substrate specificity was in the order CTP > UTP > GTP > ATP. When Mg2+ was used, the triphosphates were approximately equally good substrates. ATP hydrolytic activity was very similar with Ca2+ or Mg2+ as the cofactor, whereas Ca2+ was the more potent activator of hydrolysis of the other triphosphates tested. The preparation showed some activity toward the nucleoside diphosphates but none toward the monophosphates or p-nitrophenylphosphate. The enzymic properties of ATP hydrolysis were more closely studied. The hydrolysis was optimal at 18--24 degrees C in the presence of 1 mM-Ca2+ or 1 mM-Mg2+. Ca2+- and Mg2+-ATP hydrolysis displayed pH maxima around 8.0--8.5 and 7.4--8.0, respectively. Vmax values for Ca2+- and Mg2+-ATP hydrolysis similar: approx. 12 mumol Pi per h per mg protein with a Km value of approx. 0.05 mM. The ATP hydrolysis activity was inhibited by NaF but unaffected by ouabain, vanadate, cytochalasin B, and various drugs known to influence ATPase activity of mitochondria. Zn2+ stimulated the ATP hydrolysis activity at low concent...Continue Reading

References

Sep 1, 1976·Archives of Biochemistry and Biophysics·J D Robinson
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Nov 1, 1979·Journal of Neurochemistry·M WallinA Edström
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Apr 28, 1978·Biochemical and Biophysical Research Communications·T KobayashiM Flavin
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Jun 1, 1961·Journal of Biochemistry·F HUIJING, E C SLATER

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Citations

Apr 25, 1986·Biochimica Et Biophysica Acta·M KanjeM Wallin
Nov 1, 1984·Journal of Neurochemistry·P Ekström, M Kanje
Sep 1, 1982·Journal of Neurochemistry·L Larivière, P A Lavoie
Apr 1, 1983·Neurochemical Research·J D DohertyE G Trams

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