Crossref journal-article
Wiley
Journal of Neurochemistry (311)
Abstract

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.

Bibliography

Benjamins, J. A., & Agranoff, B. W. (1969). DISTRIBUTION AND PROPERTIES OF CDP‐DIGLYCERIDE:INOSITOL TRANSFERASE FROM BRAIN1. Journal of Neurochemistry, 16(4), 513–527. Portico.

Authors 2
  1. Joyce A. Benjamins (first)
  2. B. W. Agranoff (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 4, 2006, 10:12 p.m.)
Deposited 1 year, 10 months ago (Nov. 4, 2023, 7:44 a.m.)
Indexed 1 year, 3 months ago (May 17, 2024, 4:14 p.m.)
Issued 56 years, 5 months ago (April 1, 1969)
Published 56 years, 5 months ago (April 1, 1969)
Published Online 18 years, 11 months ago (Oct. 4, 2006)
Published Print 56 years, 5 months ago (April 1, 1969)
Funders 0

None

@article{Benjamins_1969, title={DISTRIBUTION AND PROPERTIES OF CDP‐DIGLYCERIDE:INOSITOL TRANSFERASE FROM BRAIN1}, volume={16}, ISSN={1471-4159}, url={http://dx.doi.org/10.1111/j.1471-4159.1969.tb06850.x}, DOI={10.1111/j.1471-4159.1969.tb06850.x}, number={4}, journal={Journal of Neurochemistry}, publisher={Wiley}, author={Benjamins, Joyce A. and Agranoff, B. W.}, year={1969}, month=apr, pages={513–527} }