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• W2090904224 abstract "The responses of ATPase activities to octanol and ascorbic acid have been useful in showing variations in properties of these enzymes from different tissues and from different subcellular particles or structures from a single tissue. The response of Na-K ATPase activity to low concentrations of octanol was quite different between olfactory tissue and brain subcellular particle preparations. At a concentration of approx. 0.4 mM octanol, the Na-K ATPase from olfactory tissue showed a definite stimulation of specific activity. For similar preparations from brain homogenates, the Na-K ATPase activity was inhibited at 0.4 mM octanol. At higher octanol concentrations the Na-K ATPase was strongly inhibited in preparations from both tissues. The Na-K ATPase activity was inhibited by ascorbic acid and the responses were similar for both olfactory tissue and brain preparations. There were differences in response to octanol and ascorbic acid by Mg2+ ATPase. However, for this enzyme, the differences were between subcellular fractions; similar preparations from brain and olfactory tissue had similar responses of Mg2+ ATPase to octanol and ascorbic acid. Octanol caused stimulation of the mitochondrial but inhibition of nonmitochondrial Mg2+ ATPase activities. Ascorbic acid caused stimulation of nonmitochondrial but had little or no effect on mitochondrial Mg2+ ATPase. The octanol stimulating effect on olfactory tissue Na-K ATPase was further enhanced by NaI treatment but eliminated by lubrol WX solubilization of subcellular particle preparations. However, lubrol solubilization did not effect the ascorbic acid stimulation of the Mg2+ ATPase. The use of oligomycin in conjunction with octanol and ascorbic acid on a liver mitochondrial preparation was useful in understanding the results obtained on olfactory tissue and brain preparations." @default.
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• W2090904224 date "1972-02-01" @default.
• W2090904224 modified "2023-09-23" @default.
• W2090904224 title "Biochemical studies of olfactory tissue: Responses of ATPase activities to octanol and ascorbic acid" @default.
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• W2090904224 doi "https://doi.org/10.1016/0009-2797(72)90014-2" @default.
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