منابع مشابه
Further studies with xanthine oxidase inhibitors.
The osidase and dehydrogenase activities in the enzymes oxidizing xanthine can be differentiated by the use of certain inhibitors (1). The present study was designed to see if such inhibitors are specific for the reaction with oxygen, or whether these agents also block the transfer of electrons to cytochrome c and nitrate. Both reduced diphosphopyridine nucleotide and hypoxanthine were studied ...
متن کاملRecent mechanistic studies of xanthine oxidase.
Introduction The molybdenum-containing hydroxylases constitute one of the three major categories of mononuclear molybdenum enzymes. In comparison with other biological hydroxylation systems they are unique in that they utilize water rather than dioxygen as the ultimate source of the oxygen atom incorporated into product, and generate rather than consume reducing equivalents in the course of tur...
متن کاملRecent studies on xanthine oxidase and related enzymes.
Chemistry and Biochemistry of Flavoenzymes (Muller, F., ed.), vol. 111, pp. 309-317, CRC Press, Boca Raton 7 Ratti, S., Curti, B., Zanetti, G. and Galli, E. (1985) J. Bacteriol. 163, 724-729 8 Vanoni, M. A., Negri, A., Zanetti, G., Ronchi, S. and Curti, B. (1990) Biochem. Biophys. Acta 1039, 374-377 9 Vanoni, M. A., Nuzzi, L., Rescigno, M., Zanetti, G. and Curti, B. (1991) Eur. J. Biochem. 202,...
متن کاملStudies on xanthine oxidase during carcinogenesis by p-dimethylaminoazobenzene.
Protein and riboflavin deficiencies (11, 17, 1, 7) seem to be major dietary factors involved in the production of liver cancers by feeding p-dimethylaminoazobenzene. The quantity and type of fat in the diet also appear to be important in this process (14, 18), and other dietary factors, such as biotin, play a role under certain conditions (8, 22). Con versely, a major effect of feeding p-dimeth...
متن کاملStudies on the mechanism of action of xanthine oxidase.
Recent studies of the reaction mechanism of the molybdenum-containing enzyme xanthine oxidase are presented. The pH-dependence of both the steady-state and rapid reaction kinetics of the enzyme exhibits is bell-shaped, with pK(a)s for the acid and alkaline limbs of 6.6 and 7.4, respectively. These are assigned to ionizations of an active site base and substrate, respectively, with the implicati...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1924
ISSN: 0306-3283
DOI: 10.1042/bj0180976