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A novel pathway for phosphatidylcholine catabolism in rat brain homogenates.

作者信息

Abra R M, Quinn P J

出版信息

Biochim Biophys Acta. 1975 Mar 24;380(3):436-41. doi: 10.1016/0005-2760(75)90111-3.

Abstract

Rat brain homogenates incubated with exogenous [32-P] phosphatidylcholine liberated: LYSO[32-P] phosphatidylcholine, sn-glycero-3-[32-P] phosphorylcholine, [32-P] phosphorylcholine, sn-gleycero-3-[32-P] phosphate and 32-Pi. Further investigation showed that [32-P] phosphorylcholine was released exclusively from sn-glycero-3-[32-P] phosphorylcholien by a novel diesterase activity. We propose that the enzyme be termed L-3-glycerylphosphinicocholine cholinephosphohydrolase (EC 3.1.4.-). Parallel experiments on rat liver homogenates and a P815Y mouse mastocytoma cell-lysate, revealed no diesterase activity.

摘要

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