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Title: Purification and characterization of rat liver microsomal beta-glucuronidase. Author: Owens JW, Stahl P. Journal: Biochim Biophys Acta; 1976 Jul 08; 438(2):474-86. PubMed ID: 8108. Abstract: Beta-Glucuronidase (EC 3.2.1.31) has been isolated from rat-liver microsomes by a novel chromatographic method employing antibody to rat preputial gland beta-glucuronidase coupled to Sepharose. The purified enzyme, homogeneous by several methods, was purified some 1700-fold. The microsomal beta-glucuronidase has been characterized with respect to catalysis, stability, and molecular weight. The purified enzyme is a tetramer of 290 000 daltons. Comparative studies with lysosomal beta-glucuronidase indicate that while these two enzymes are electrophoretically distinct, they are catalytically and immunologically identical and have indistinguishable molecular dimensions. The results suggest that microsomal and lysosomal beta-glucuronidase are charge isomers.[Abstract] [Full Text] [Related] [New Search]