RAPID PARTIAL-PURIFICATION OF PLACENTAL GLUCOCEREBROSIDE BETA-GLUCOSIDASE AND ITS ENTRAPMENT IN LIPOSOMES
RAPID PARTIAL-PURIFICATION OF PLACENTAL GLUCOCEREBROSIDE BETA-GLUCOSIDASE AND ITS ENTRAPMENT IN LIPOSOMES
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DOI:
10.1042/bj1640439
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发表时间:
1977-01-01
影响因子:
4.1
通讯作者:
GREGORIADIS, G
中科院分区:
文献类型:
--
作者:
BRAIDMAN, IP;GREGORIADIS, G
A glucocerebroside .beta.-glucosidase-rich detergent-free preparation was obtained from human placentas by a rapid method combining affinity chromatography on concanavalin A-Sepharose and organic-solvent precipitation. In a typical preparation about 11,000 units of the enzyme purified 1500-fold were obtained from 5 placentas in 2 days. The enzyme preparation also contained other hydrolases, but the extent of their purification was much smaller. Studies on entrapment in liposomes showed that all glucocerebroside .beta.-glucosidase activity used was incorporated in neutral egg phosphatidylcholine-cholesterol liposomes. Association with liposomes discriminated against other proteins, including some of the hydrolases, thus contributing to further purification of the enzyme. More than 95% of the liposome-associated enzyme activity was latent.