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A more recent version of this article appeared on October 5, 2001
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M104290200v1
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Papers In Press, published online ahead of print August 6, 2001
J. Biol. Chem, 10.1074/jbc.M104290200
Submitted on May 11, 2001
Revised on August 6, 2001
Accepted on August 6, 2001

Molecular cloning and expression of human bile acid beta-glucosidase

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

Internal Medicine III, RWTH Aachen, Aachen 52057

Corresponding Author: MK3{at}post.klinikum.rwth-aachen.de

A novel microsomal beta-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 beta-glucosidase was now 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 Mr of 104,648 containing one putative transmembrane domain. Database searches revealed no homology with any other known protein, but showed occurrence of the cDNA sequence 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 beta-glucosidase activity. Northern blot analysis of various human tissues revealed high levels of expression of the bile acid beta-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.


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