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J. Biol. Chem., Vol. 276, Issue 41, 37929-37933, October 12, 2001

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Molecular Cloning and Expression of Human Bile Acid -Glucosidase^*

Heidrun Matern, Henrike Boermans, Friedrich Lottspeich^§, and Siegfried Matern

From the Department of Internal Medicine III, Rheinisch-Westfälische Technische Hochschule Aachen, 52057 Aachen, Germany and ^§ Genzentrum Martinsried, 82152 Martinsried, Germany

A novel microsomal -glucosidase was recently purified and characterized from human liver that catalyzes the hydrolysis of bile acid 3-O-glucosides as endogenous compounds. The primary structure of this bile acid -glucosidase was deduced by cDNA cloning on the basis of the amino acid sequences of peptides obtained from the purified enzyme by proteinase digestion. The isolated cDNA comprises 3639 base pairs containing 524 nucleotides of 5'-untranslated and 334 nucleotides of 3'-untranslated sequences including the poly(A) tail. The open reading frame predicts a 927-amino acid protein with a calculated M_r of 104,648 containing one putative transmembrane domain. Data base searches revealed no homology with any known glycosyl hydrolase or other functionally identified protein. The cDNA sequence was found with significant identity in the human chromosome 9 clone RP11-112J3 of the human genome project. The recombinant enzyme was expressed in a tagged form in COS-7 cells where it displayed bile acid -glucosidase activity. Northern blot analysis of various human tissues revealed high levels of expression of the bile acid -glucosidase mRNA (3.6-kilobase message) in brain, heart, skeletal muscle, kidney, and placenta and lower levels of expression in the liver and other organs.

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBank^TM/EBI Data Bank with accession number(s) AJ309567.

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