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- W2057067739 abstract "Abstract A transacylase that converts 1-palmitoyl lysophosphatidylcholine to dipalmitoyl phosphatidylcholine was demonstrated in the rat gastric mucosa. This enzyme required neither ATP or CoA nor bile salt and detergent for its activity. The enzyme preparation also exhibited powerful lysophospholipase activity. The transacylase and lysophospholipase were both located in the cytosol fraction, and their activities remained associated at a constant ratio throughout the purification steps, including the isoelectrofocusing procedure. They responded similarly with respect to the addition of metal ions, bile salt, detergent, and heat treatment. Both enzyme activities also exhibited similar apparent K m values for lysophosphatidylcholine. These observations suggest that both the lysophospholipase and transacylase activities may reside in the same enzyme." @default.
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- W2057067739 date "1979-03-01" @default.
- W2057067739 modified "2023-09-27" @default.
- W2057067739 title "Lysophospholipase and transacylase activities of rat gastric mucosa" @default.
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- W2057067739 doi "https://doi.org/10.1016/0003-9861(79)90025-0" @default.
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