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. 1993 Dec;10(6):447-52.
doi: 10.1007/BF00737965.

Action of alpha-L-fucoside from Octopus vulgaris hepatopancreas on phospholipid vesicles containing the fucosylated ganglioside FucGM1

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Action of alpha-L-fucoside from Octopus vulgaris hepatopancreas on phospholipid vesicles containing the fucosylated ganglioside FucGM1

A Giuliani et al. Glycoconj J. 1993 Dec.

Abstract

The behaviour of a highly purified alpha-L-fucosidase (E.C. 3.2.1.51) extracted from octopus hepatopancreas was studied with phospholipid vesicles composed of phosphatidylcholine (PC) and phosphatidylserine (PS) containing the fucosylated ganglioside FucGM1, a potential natural substrate of the enzyme. The substrate recognition and hydrolysis take place only with PS/FucGM1 mixtures via an association process of the enzyme with the vesicles at acidic pH; the enzyme rapidly and stably binds to PS vesicles but not to PC vesicles. The data suggest that only the PS-associated enzyme is able to hydrolyse FucGM1 embedded in the same bilayer. The enzyme association with FucGM1/PS vesicles is a prerequisite for ganglioside hydrolysis but is followed by irreversible enzyme inactivation.

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