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DISTRIBUTION AND PROPERTIES OF CDP‐DIGLYCERIDE:INOSITOL TRANSFERASE FROM BRAIN 1
Author(s) -
Benjamins Joyce A.,
Agranoff B. W.
Publication year - 1969
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.1471-4159.1969.tb06850.x
Subject(s) - inositol , chemistry , biochemistry , microsome , substrate (aquarium) , enzyme , transferase , diglyceride , guinea pig , stereochemistry , chromatography , biology , receptor , ecology , endocrinology
Abstract— CDP‐diglyceride is converted to phosphatidyl inositol by several particulate subcellular fractions of guinea pig brain, with highest specific activity in the microsomal fraction. Optimal conditions with respect to pH, metal ion concentration, and substrate concentrations have been determined. The reaction was stimulated by the addition of bovine serum albumin and by Tween 80. Of several dl ‐CDP‐diglycerides synthesized and used as substrates in a spectrophoto‐metric assay for the enzyme, dl ‐CDP‐didecanoin was the most active. The enzyme showed a high selectivity for myo‐inositol. Of a number of compounds tested, only scyllo ‐inosose and epi ‐inosose served as substrates. Three inositol isomers and three myo ‐inositol monophosphates inhibited the reaction slightly. The most potent inhibitor found was galactinol, a myo ‐inositol galactoside.