Purification of a phosphatidic-acid-hydrolysing phospholipase A2 from rat brain

Thomson, F. J. and Clark, M. A. (1995) Purification of a phosphatidic-acid-hydrolysing phospholipase A2 from rat brain. Biochemical Journal, 306(1), pp. 305-309. (PMID:7864824)

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A phosphatidic-acid-hydrolysing phospholipase A2 was purified from rat brain and characterized. This phospholipase A2 was purified by sequential cation, hydrophobic, heparin and gel-filtration chromatography. The purified protein had a mass of approximately 58 kDa as assayed by SDS/PAGE, had a pH optimum of 6.0, and was Ca(2+)-independent. This enzyme was apparently phosphatidic-acid-selective and had little measurable catalytic activity when phosphatidylcholine, phosphatidylethanolamine or diacylglycerol was used as substrate. On the basis of its physical and catalytic properties, we conclude that this phospholipase A2 is unique from those previously purified, and we speculate that it may be important for the production of the bioactive lipid lysophosphatidic acid.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Thomson, Dr Fiona
Authors: Thomson, F. J., and Clark, M. A.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Biochemical Journal
Publisher:Portland Press Ltd.
ISSN (Online):1470-8728

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