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. 1990 Apr 15;267(2):423–429. doi: 10.1042/bj2670423

Effect of pH on the activity of the Ca2+ + Mg2(+)-activated ATPase of sarcoplasmic reticulum.

F Michelangeli 1, J Colyer 1, J M East 1, A G Lee 1
PMCID: PMC1131306  PMID: 2139777

Abstract

A kinetic model for the Ca2(+) + Mg2(+)-activated ATPase of sarcoplasmic reticulum was presented in a previous paper [Stefanova, Napier, East & Lee (1987) Biochem. J. 245, 723-730]. Here, that model is modified to account for the pH-dependence of ATPase activity and for the effects of Mg2+ on activity at high pH. It is shown that effects of Mg2+ on measurements of ATPase activity as a function of ATP concentration at pH 8.0 and pH 8.5 are consistent with binding of Mg2+ to the Ca2(+)-binding sites on the phosphorylated ATPase, such binding inhibiting dephosphorylation of the ATPase. It is also shown that slow dissociation of Ca2+ from the phosphorylated ATPase is consistent with the previously published model.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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