ON THE PHOSPHOLIPASE A2 ACTIVITY OF HUMAN CEREBRAL CORTEX |
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| Authors: | Mary F Cooper G R Webster |
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| Institution: | Department of Chemical Pathology, Guy's Hospital Medical School, London S.E.1, Great Britain |
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| Abstract: | Abstract— Preparations of phospholipase Az have been obtained from human cerebral cortex. The enzyme was extracted from acetone-dried tissue and purified by heat-treatment and gel filtration on Sephadex.
Although heating at 65°C or 70°C destroys most of the phospholipase A1 activity that is present in crude extracts, a small proportion remains associated with the A2 activity during these procedures. The heat-treated extracts hydrolyse lecithin in preference to phosphatidyl-ethanolamine but have no action on lysolecithin or neutral lipids. The results suggest that A2 activity and the heat-stable component of A1 may both be due to a single phospholipase A that can hydrolyse diacylglycerophosphatides at either the 2-or the 1-position, to form a mixture of isomeric lysoderivatives.
A molecular weight of 55,000 was calculated for the enzyme. |
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