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Title: On the functional heterogeneity of UDP-glucuronyl transferase of mouse liver microsomes. Author: Bansal SK, Li HC, Holmes G, Gessner T. Journal: Res Commun Chem Pathol Pharmacol; 1982 Feb; 35(2):291-302. PubMed ID: 6803311. Abstract: Fractionation of sodium cholate solubilized microsomes from mouse liver on Sepharose CL-48 yielded three protein peaks with UDP-glucuronyltransferase activities. Of these three peaks, only peak II contained activities towards all the substrates tested: p-nitrophenol, 1-naphthol, morphine, testosterone and estrone. These glucuronyltransferase activities could not be dissociated by further chromatography on DEAE-Sepharose CL-6B and isoelectric focusing. The results show the presence of a functional form of glucuronyltransferase with a wide substrate specificity, and indicate that in addition, other forms with narrower studied specificities may also be present in mouse liver microsomes.[Abstract] [Full Text] [Related] [New Search]