A model for the phosphorylation of the Ca2+ + Mg2+-activated ATPase by phosphate.
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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+.
SUBMITTER: Froud RJ
PROVIDER: S-EPMC1146967 | biostudies-other | 1986 Jul
REPOSITORIES: biostudies-other
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