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Hydrolysis of Galactose from Glycolipids and Glycoprotein by Young Rat Brain β‐Galactosidases Immobilized to Sepharose 4B
Author(s) -
Yeung KwokKam,
McKinney Richard A.,
Dain Joel A.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb06279.x
Subject(s) - galactosidases , hydrolysis , sepharose , chemistry , biochemistry , cyanogen bromide , chromatography , galactose , lactose , glycolipid , ganglioside , enzyme , glycosidic bond , enzymatic hydrolysis , beta galactosidase , substrate (aquarium) , biology , peptide sequence , gene , ecology , gene expression
An extract of glycosidic enzymes from young rat brain was immobilized to cyanogen bromide‐activated Sepharose 4B. Most glycosidases retained approximately 10‐25% of their activities after immobilization. Immobilized β‐galactosidases were used repeatedly without detectable loss of enzyme activity in the hydrolysis of p ‐nitrophenyl‐β‐ d ‐galactopyranoside. In addition to the synthetic substrate, the immobilized rat brain β‐galactosidases could also hydrolyze galactose from lactose, galactosylcerebroside, asialofetuin, and GM 1 ‐ganglioside. The hydrolysis of GM 1 ‐ to GM 2 ‐ganglioside was confirmed on TLC.