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• W2163125220 abstract "The effects of the three hydrophobic molecules triphenylphosphine, trifluoperazine and 3-nitrophenol on Ca2+ uptake and ATPase activity in sarcoplasmic reticulum vesicles was investigated. When ATP was the substrate, triphenylphosphine (3 μM) increased the amount of Ca2+ accumulated by the vesicles. At high concentrations triphenylphosphine inhibited Ca2+ uptake. This effect varied depending on the ATP concentration and the type of nucleotide used. With ITP there was only inhibition and no activation of Ca2+ uptake by triphenylphosphine. On the other hand, trifluoperazine inhibited Ca2+ accumulation regardless of whether ATP or ITP was used as substrate. When 5 mM oxalate was included in the medium in order to avoid binding of Ca2+ to the low-affinity Ca2+-binding sites of the enzyme, both stimulation by triphenylphosphine and inhibition by trifluoperazine were reduced. In leaky vesicles at low Ca2+ concentrations, triphenylphosphine and 3-nitrophenol were competitive inhibitors of ATPase activity at the regulatory site of the enzyme (0.1–1 mM ATP). A striking difference was observed when both the high- and low-affinity Ca2+-binding sites were saturated. In this condition, triphenylphosphine and 3-nitrophenol promoted a 3–4 fold increase in the apparent affinity for ATP at its regulatory site." @default.
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• W2163125220 date "1990-11-01" @default.
• W2163125220 modified "2023-09-26" @default.
• W2163125220 title "Modification of ATP regulatory function in sacroplasmic reticulum Ca2+-ATPase by hydrophobic molecules" @default.
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• W2163125220 doi "https://doi.org/10.1111/j.1432-1033.1990.tb19411.x" @default.
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