Purification and characterization of a microsomal bile acid β-glucosidase from human liver
H Matern, H Heinemann, G Legler, S Matern - Journal of Biological …, 1997 - ASBMB
A human liver microsomal β-glucosidase has been purified to apparent homogeneity in
sodium dodecyl sulfate-polyacrylamide gel electrophoresis where a single protein band of M
r 100,000 was obtained under reducing conditions. The enzyme was enriched about 73,000-
fold over starting microsomal membranes by polyethylene glycol fractionation, anion
exchange chromatographies on DEAE-Trisacryl, and Mono Q followed by affinity
chromatography on N-(9-carboxynonyl)-1-deoxynojirimycin-AH-Sepharose 4B. The purified …
sodium dodecyl sulfate-polyacrylamide gel electrophoresis where a single protein band of M
r 100,000 was obtained under reducing conditions. The enzyme was enriched about 73,000-
fold over starting microsomal membranes by polyethylene glycol fractionation, anion
exchange chromatographies on DEAE-Trisacryl, and Mono Q followed by affinity
chromatography on N-(9-carboxynonyl)-1-deoxynojirimycin-AH-Sepharose 4B. The purified …
