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- W1808185762 abstract "We previously showed that A23187 in high ionophore/protein ratios almost completely inhibits the sarcoplasmic reticulum Ca2+-ATPase [Hara, H. & Kanazawa, T. (1986) J. BioL Chem 261, 16584–16690]. In an attempt to obtain information on the mechanism of this inhibition, the effects of A23187 on conformational changes involved in the Ca2+-induced activation of the enzyme were investigated. The purified enzyme from sarcoplasmic reticulum of rabbit skeletal muscle as well as the purified enzyme labeled with fluorescein 5-isothiocyanate (FITC) were preincubated with A23187 in the absence of Ca2+ at pH 7.0 and O°C for 45 min. The activation of the enzyme following addition of CaCl2 was assessed by determining the capacity for rapid formation of phosphoenzyme from ATP. This activation was strongly inhibited by the preincubation with A23187. This indicates that the previously observed inhibition of the Ca2+-ATPase is mostly due to hindrance of the Ca2+-induced activation of the enzyme. In the control, in which the FITC-labeled enzyme was preincubated without A23187, the fluorescence intensity of the bound FITC decreased in a biphasic manner upon addition of CaCl2. The first rapid phase of this fluorescence drop was unaffected by A23187, whereas its second slow phase was almost completely inhibited by this drug. These results show that the Ca2+-dependent conformational change is biphasic and that the second slow phase (but not the first rapid phase) of this conformational change is inhibited by A23187. This suggests that the observed inhibition of Ca2+ activation is attributed to hindrance of the second slow phase of the Ca2+-dependent conformational change." @default.
- W1808185762 created "2016-06-24" @default.
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- W1808185762 date "1991-05-01" @default.
- W1808185762 modified "2023-10-07" @default.
- W1808185762 title "Inhibition by A23187 of Conformational Changes Involved in the Ca2+-Induced Activation of Sarcoplasmic Reticulum Ca2+-ATPase1" @default.
- W1808185762 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a123452" @default.
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