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Metal ion stimulation of phospholipase D‐like activity of isolated rat intestinal mitochondria
Author(s) -
Madesh M.,
Balasubramanian K. A.
Publication year - 1997
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-997-0061-9
Subject(s) - phosphatidylethanolamine , phosphatidic acid , phospholipase d , phosphatidylcholine , phosphatidylethanol , chemistry , phospholipid , biochemistry , phospholipase a1 , phospholipase , enzyme , enzyme assay , substrate (aquarium) , hydrolysis , chromatography , biology , ecology , membrane
Presence of phospholipase D‐like (PLD) activity in the intestinal mitochondria was identified using endogenous phospholipids as substrate. The enzyme had a pH optimum of 6.5, did not show trans ‐phosphatidylation activity in the presence of ethanol or butanol, and the product formed was phosphatidic acid (PA). This was confirmed by separation of reaction products by high‐performance liquid chromatography and analysis of composition of the PA formed which gave phosphate/fatty acid ratio of 1∶2. PLD‐like activity was further confirmed by the formation of ethanolamine and choline as products of enzyme action. This activity was stimulated by various metal ions; when stimulated by Mg 2+ and Ba 2+ , it hydrolyzed both phosphatidylcholine and phosphatidylethanolamine, and when stimulated by Ca 2+ , it preferentially hydrolyzed phosphatidylethanolamine. There was no requirement for sodium oleate for the PLD‐like activity in mitochondria. These results suggest that intestinal mitochondria have an active PLD‐like enzyme which differs in certain properties from phospholipase D from other tissues.