Selectivity of acyl transfer between phospholipids: arachidonoyl transacylase in dog heart membranes |
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Authors: | P V Reddy H H Schmid |
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Institution: | 1. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan;2. World Intec Co., Ltd., Fukuoka 812-0011, Japan |
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Abstract: | Dog heart microsomes catalyze the transfer of acyl groups from the sn-2 position of exogenous phosphatidylcholine to 1-acyl lysophosphatidylethanolamine. Approximately equal amounts of free fatty acids are produced as well. The reaction exhibits a pH optimum of 7.5-8.5 and does not require Ca2+ or other divalent cations. The reaction proceeds in the absence of exogenous coenzyme A but acyl transfer is enhanced by its addition. The transacylase exhibits a strong preference for arachidonate over linoleate and thus may be involved in the maintenance of the high amounts of arachidonate found in microsomal ethanolamine phospholipids. |
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