Biochimica et Biophysica Acta (BBA) - General Subjects
Distribution of xanthine dehydrogenase and oxidase activities in human and rabbit tissues
References (49)
- et al.
J. Mol. Cell Cardiol.
(1987) - et al.
Comp. Biochem. Physiol.
(1974) - et al.
Clin. Chim. Acta
(1965) - et al.
J. Biol. Chem.
(1961) - et al.
J. Biol. Chem.
(1969) Dev. Biol.
(1973)- et al.
Am. J. Obstet. Gynec.
(1964) - et al.
Biochem. Biophys. Res. Commun.
(1986) - et al.
Arch. Biochem. Biophys.
(1978) N. Engl. J. Med.
(1985)
Clin. Sci.
Ped. Res.
Acta Physiol. Scand. Suppl.
Am. J. Physiol.
Clin. Res.
Brain Energy Metabolism
Biochem. J.
J. Clin. Invest.
J. Lab. Clin. Med.
Enzyme
J. Lab. Clin. Med.
J. Neurochem.
Biochem. Med.
J. Clin. Pathol.
Cited by (96)
Comprehensive analysis of mechanism underlying hypouricemic effect of glucosyl hesperidin
2020, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Therefore, it remains unclear whether GH can be expected to have similar hypouricemic activity to such drugs in humans. However, our results show that GH inhibited XOD activity and decreased SUAs in mice, whose XOD activity is approximately 100 times higher than that of humans [29,30]. Therefore, GH’s inhibition of XOD activity could also be efficacious against hyperuricemia in humans.
The cellular and molecular origin of reactive oxygen species generation during myocardial ischemia and reperfusion
2012, Pharmacology and TherapeuticsCitation Excerpt :These secondary effects are more likely explanations for allopurinol-mediated protective effects recently reported in patients undergoing percutaneous intervention following acute myocardial infarction (Rentoukas et al., 2010). Xanthine dehydrogenase activity was found to be relatively stable in human heart tissue (Wajner & Harkness, 1989), and its conversion to xanthine oxidase is a relatively slow process with a half-life of 7 h in ischemic rat tissue (Engerson et al., 1987). This xanthine dehydrogenase stability suggests that xanthine oxidase is unlikely to be appreciably formed during transient ischemia.
The significance of serum xanthine oxidase and oxidation markers in acute paraquat poisoning in humans
2011, Clinical BiochemistryDetermination of xanthine oxidoreductase activity in broilers: Effect of pH and temperature of the assay and distribution in tissues
2009, Poultry ScienceCitation Excerpt :However, comparing absolute values of XOR activity measured in different studies is difficult because of the temperature and buffer variations in the measurements (Nishino et al., 1989). In most studies involving mammalian tissues, XOR activity has been measured at either 25°C (Rajagopalan and Handler, 1967; Wajner and Harkness, 1989) or 37°C (Terada et al., 1990; Saksela and Raivio, 1996). In studies involving avian tissues, the activity of XOR has been measured at 25°C (Strittmatter, 1965; Nishino et al., 1989; Sato et al., 1995), 30°C (Bruguera et al., 1988), 38°C (Remy et al., 1955), or 41°C (Scholz and Featherston, 1968).
- *
Present address: Dept. Bioquimica, Instituto de Biociencias, UFRGS, Rua Sarmento Leite s/n, 90.050 Porto Alegre RS, Brasil.