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EFFECTS OF ETHANOL ON THE ACTIVITY OF ADENOSINE TRIPHOSPHATASE AND ACETYLCHOLINESTERASE IN SYNAPTOSOMES ISOLATED FROM GUINEA‐PIG BRAIN
Author(s) -
Sun A. Y.,
Samorajski T.
Publication year - 1970
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1970.tb06871.x
Subject(s) - acetylcholinesterase , atpase , guinea pig , chemistry , ethanol , synaptosome , adenosine triphosphatase , aché , biochemistry , triphosphatase , adenosine , enzyme , membrane , endocrinology , biology
— 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.