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- W2466983918 abstract "Alkaline phosphatase is anchored to the plasma membrane by a carboxyl-terminal phosphatidylinositol glycan moiety. To investigate the biosynthesis of mature alkaline phosphatase, nascent human placental alkaline phos- phatase was expressed in a cell-free system and used as substrate for in vitro processing by microsomal extracts. By monitoring the processed product with three site-directed antibodies, it was shown that microsomal extracts from CHO cells that contain other recognized processing activities also remove the carboxyl-terminal signal peptide from the pre- proenzyme in an apparently selective manner. This peptidase- like cleavage may be brought about by the action of a specific transamidase acting on the nascent protein in the absence of an appropriate phosphatidylinositol glycan cosubstrate." @default.
- W2466983918 created "2016-07-22" @default.
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- W2466983918 date "2016-01-01" @default.
- W2466983918 modified "2023-09-27" @default.
- W2466983918 title "Processing at the carboxyl terminus of nascent placental alkaline phosphatase in a cell-free system: Evidence for specific cleavage of a signal peptide (membrane-anchored proteins/phosphatidylinositol glycan)" @default.
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- W2466983918 hasPublicationYear "2016" @default.
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