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- W2041655276 abstract "Nerve ending fractions from guinea-pig cerebral cortex contained more than one-half of the Na-K ATPase activity present in the original homogenate. Ethanol at concentrations ranging from 0·043 to 2·57 m inhibited the Na-K ATPase to a significantly greater extent than the Mg-activated ATPase or AChE. The inhibition of membrane-bound Na-K ATPase by ethanol was of the non-competetive type and the activity of Na-K ATPase was increasingly inhibited by alcohols of increasingly longer chain length. The ability of various alcohols to inhibit membrane-bound Na-K ATPase activity was correlated with their lipid solubility." @default.
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- W2041655276 date "1970-09-01" @default.
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- W2041655276 title "EFFECTS OF ETHANOL ON THE ACTIVITY OF ADENOSINE TRIPHOSPHATASE AND ACETYLCHOLINESTERASE IN SYNAPTOSOMES ISOLATED FROM GUINEA-PIG BRAIN" @default.
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- W2041655276 doi "https://doi.org/10.1111/j.1471-4159.1970.tb06871.x" @default.
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