PMID: 7087686Feb 1, 1982Paper

On the specificity of a phospholipase A2 purified from the 106,000 X g pellet of bovine brain

N C Gray, K P Strickland


Assessment has been made of the specificity of a purified phospholipase A2 from the 106,000 X g pellet (microsomal fraction) of bovine grey matter which shows strong activity toward phosphatidylinositol (PI). In the first series of experiments involving the utilization as substrates of PI with different 14C- or 3H-labeled fatty acids in the 2-position, the purified phospholipase A2 most readily removed 16:0 palmitic acid, followed by 18:0 stearic acid, 18:1 oleic acid and 20:4 arachidonic acid. In the second series of experiments, the purified phospholipase A2 showed preferential action toward PI (100%) compared to phosphatidylcholine (PC, 62.5%), phosphatidic acid (PA, 32.6%), phosphatidylethanolamine (PE, 25.1%) and phosphatidylserine (PS, 21.5%), where each phosphoglyceride was labeled in the 2-position with [1-14C] oleic acid. In the third series of experiments, fatty acids were shown to cause inhibition of action of the purified phospholipase A2 on 1-acyl, 2-[1-14C] oleoyl PI in the order 20:4 greater than 18:1 greater than 18:0 greater than 16:0 which is the reverse order to that just noted. In the final series of experiments, the addition of the phosphoglycerides PC, PE, PS and PA in amounts of 5 or 10 microM caused eith...Continue Reading


Dec 1, 1979·Canadian Journal of Biochemistry·T Y ShumK P Strickland
Apr 26, 1977·Biochimica Et Biophysica Acta·B Haye, C Jacquemin
Jan 1, 1974·Annual Review of Biochemistry·H van den Bosch
Mar 16, 1971·Biochimica Et Biophysica Acta·A MontfoortL L van Deenen
Jan 1, 1964·The Biochemical Journal·G R Webster, R J Alpern
Sep 30, 1980·Biochimica Et Biophysica Acta·H van den Bosch

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