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. 1983;2(9):1543–1548. doi: 10.1002/j.1460-2075.1983.tb01621.x

Activation of sarcoplasmic reticular Ca2+ transport ATPase by phosphorylation of an associated phosphatidylinositol.

M Varsanyi 1, H G Tölle 1, M G Heilmeyer Jr 1, R M Dawson 1, R F Irvine 1
PMCID: PMC555320  PMID: 11892809

Abstract

Approximately 1 mol phosphatidylinositol phosphate is formed per mol isolated Ca2+ transport ATPase when the enzyme is incubated with ATP/Mg2+. The phosphorylation of this enzyme-associated phosphatidylinositol represents the alkylphosphate formation described earlier. The phosphatidylinositol phosphate has been found in the hydrophobic core of the enzyme. A complex of phosphatidylinositol phosphate with protein can be extracted with acidic chloroform/methanol. The protein behaves like proteolipid during chromatography on Sephadex LH 60 and binds the radioactively labelled phosphatidylinositol phosphate. The phosphorylation of approximately 1 mol phosphatidylinositol per 100,000 g protein correlates with an enhancement of the Ca2+ transport ATPase activity which is due to an approximately 7-fold enhanced affinity for Ca2+ and an approximately 2-fold enhanced maximal turnover.

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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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