A model for the phosphorylation of the Ca2+ + Mg2+-activated ATPase by phosphate
- 1 July 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 237 (1) , 207-215
- https://doi.org/10.1042/bj2370207
Abstract
We have shown that changes in fluorescence intensity for the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum labelled with fluorescein isothiocyanate following the addition of Ca2+ can give the ratio of the two conformations (E1 and E2) of the ATPase. We show that the fluorescence response to Ca2+ is unaffected by Mg2+, phosphate or K+, implying that these ions bind equally well to the E1 and E2 conformations. A model is presented for phosphorylation of the ATPase by phosphate as a function of pH, Mg2+, K+ and Ca2+.This publication has 27 references indexed in Scilit:
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