Open AccessEnzymic Deacylation of Lipids in Plants
Author(s) -
Galliard Terence
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01444.x
Subject(s) - phosphatidylcholine , phosphatidylethanolamine , chemistry , phospholipid , biochemistry , phosphatidic acid , fatty acid , bovine serum albumin , hydrolysis , chromatography , membrane
1 Deacylation of phosphatidylcholine by the lipolytic acyl hydrolase enzyme in homogenates of potato tubers was stimulated by endogenous free fatty acids in the homogenates. 2 Partially purified enzyme preparations were inactive in the absence of surface active agents. 3 The fatty acid‐stimulated enzymic deacylation of phosphatidylcholine showed a pH optimum between 5.5 and 6.0 and was reversed by bovine serum albumin. 4 Free fatty acids were more effective than other lipids and surface active compounds studied. 5 Long‐chain cis ‐unsaturated fatty acids were most effective. 6 Enzymic hydrolysis of phosphatidylethanolamine showed a similar stimulation by free fatty acids but hydrolysis of lyso ‐phosphatidylcholine, phosphatidylglycerol, phosphatidic acid, galactolipids or monoglycerides was not stimulated. 7 Similar stimulation by linoleic acid of the enzymic deacylation of membrane‐bound phospholipid was observed and found to be prevented by bovine serum albumin. 8 Electron microscope studies suggested that free fatty acids had a marked effect on the physical state of phosphatidylcholine in aqueous dispersions.