Purification and characterization of rat liver microsomal beta-glucuronidase.
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.
D000818:Animals; D004355:Drug Stability; D005260:Female; D005966:Glucuronidase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology; D008862:Microsomes, Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D005966:Glucuronidase