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Volume 272, Number 17, Issue of April 25, 1997 pp. 11261-11267
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Purification and Characterization of a Microsomal Bile Acid beta -Glucosidase from Human Liver

(Received for publication, September 5, 1996, and in revised form, January 29, 1997)

Heidrun Matern Dagger , Heribert Heinemann Dagger , Günter Legler and Siegfried Matern Dagger

From the Dagger  Department of Internal Medicine III, Aachen University of Technology, D-52074 Aachen and  Institut für Biochemie, Universität Köln, D-50674 Köln, Federal Republic of Germany

A human liver microsomal beta -glucosidase has been purified to apparent homogeneity in sodium dodecyl sulfate-polyacrylamide gel electrophoresis where a single protein band of Mr 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 enzyme had a pH optimum between 5.0 and 6.4, was activated by divalent metal ions, and required phospholipids for exhibition of activity. The enzyme catalyzed the hydrolysis of 3beta -D-glucosido-lithocholic and 3beta -D-glucosido-chenodeoxycholic acids with high affinity (Km, 1.7 and 6.2 µM, respectively) and of the beta -D-glucoside (Km, 210 µM) and the beta -D-galactoside of 4-methylumbelliferone. The ratio of relative reaction rates for these substrates was about 6:3:11:1. No activity was detectable toward 6beta -D-glucosido-hyodeoxycholic acid, glucocerebroside, and the following glycosides of 4-methylumbelliferone: alpha -D-glucoside, alpha -L-arabinoside, beta -D-fucoside or beta -D-xyloside. Immunoinhibition and immunoprecipitation studies using antibodies prepared against lysosomal glucocerebrosidase showed no cross-reactivity with microsomal beta -glucosidase suggesting that these two enzymes are antigenically unrelated.


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