The molecular biology of UDP-glucuronyltransferases.
نویسندگان
چکیده
Beale. D.. Ketterer. B., Carne, T., Meyer, D. & Taylor, J . B. (1982) Eur. J. Biochem. 126. 459 463 Beale. D.. Meyer, D., Taylor, J. B. & Ketterer. B. (1983) Eur. J. Biochem. 137. 125 129 Ding. G. J.-F.. Lu. A. Y. H. & Pickett, C. B. (1985) J. B i d . Chem. 260. 13268 13271 Jakoby. W. B. & Habig. W. H. (1980) in Enzymutic Basis qf DeroxiCU/ i (Jn (Jakoby. W. B., ed.), vol. 2. pp. 63--94, Academic Press, New York Ketterer. B.. Meyer, D. J., Coles, B., Taylor, J . B. & Pemble, S. E. ( 1986) in Antimu/agenesis and Anticarcinogenesis: Mechanisms (Shankel. D. M.. Hartman, P., Kada, T. & Hollaender, A,, eds.), pp. 103 126, Plenum Press, New York Lai. H.-C. J., Li. N.-Q., Weiss, M. J., Reddy. C. C. & Tu, C.-P. D . (1984) J . BifJ/. Chem. 259, 553&5542 Lai. H.-C. J.. Grove. G. & Tu, C.-P. D. (1986) Nucleic Acids Res. 14. 6101 6114 Mannervik, B. (1985) Adv. Enzymol. Relur. Areus Mol . Biol. 57,
منابع مشابه
Diazobenzenesulphonate selectively abolishes stimulation of glucuronidation by UDP-N-acetylglucosamine.
1. Basal rates of glucuronidation of oestrone (guinea pig) or of 4-nitrophenol (rat or guinea pig) were not significantly altered in sealed liver microsomal vesicles, treated with the membrane-impermeant protein-modifying agent diazobenzenesulphonate at 0.5-1.0 mM. 2. Contrarily, diazobenzenesulphonate abolished the normal stimulation of glucuronidation by UDP-N-acetylglucosamine. 3. Ultrasonic...
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The structure of the UDP-glucuronyltransferases in microsomes from guinea pig and rat liver was examined in situ by radiation inactivation analysis. The p-nitrophenol conjugating activity of guinea pig microsomes increased at lower doses of radiation; at higher doses (greater than or equal to 36 megarads), activity showed a first order decline yielding a target size of 71 +/- 9 kDa. Treating mi...
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ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 15 4 شماره
صفحات -
تاریخ انتشار 1987