TY - JOUR
T1 - Metal ion stimulation of phospholipase D-like activity of isolated rat intestinal mitochondria
AU - Madesh, M.
AU - Balasubramanian, K. A.
N1 - Funding Information:
The Wellcome Trust Research Laboratory is supported by The Wellcome Trust, London. Financial assistance from the Department of Science and Technology and Indian Council of Medical Research, Government of India, is gratefully acknowledged. The authors thank Professor V.I. Mathan for his keen interest in this work. M. Madesh is a Senior Research Fellow of the Council of the Scientific and Industrial Research India.
PY - 1997/5
Y1 - 1997/5
N2 - 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 Mg2+ and Ba2+, it hydrolyzed both phosphatidylcholine and phosphatidylethanolamine, and when stimulated by Ca2+, 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.
AB - 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 Mg2+ and Ba2+, it hydrolyzed both phosphatidylcholine and phosphatidylethanolamine, and when stimulated by Ca2+, 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.
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U2 - 10.1007/s11745-997-0061-9
DO - 10.1007/s11745-997-0061-9
M3 - Article
C2 - 9168453
AN - SCOPUS:0030968813
SN - 0024-4201
VL - 32
SP - 471
EP - 479
JO - Lipids
JF - Lipids
IS - 5
ER -