The Nature of the Xanthine Oxidase Factor

Renzo, E.C. De; Kaleita, E.; Heytler, Peter G.; Oleson, J. J.; Hutchings, B. L.; Williams, J. H.

doi:10.1021/ja01099a515

Cited by 64 publications

(15 citation statements)

References 3 publications

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“…Parallel decreases in myocardial XO activity, ventricular dysfunction, and H202 generation occurred in tungsten-or allopurinol-treated rats subjected to ischemia and then reperfusion. Tungsten is a relatively specific inhibitor that inactivates xanthine, aldehyde, and sulfite oxidases by interfering with their molybdenum-dependent active site (7)(8)(9). By comparison, allopurinol and its metabolite oxipurinol are potent, specific competitive inhibitors of XO (10), but not sulfite or aldehyde oxidases.…”

Section: Discussionmentioning

confidence: 99%

“…We tested this premise in simplified ("blood-free") isolated hearts using dimethylthiourea (DMTU), a highly permeant 02 metabolite scavenger, infused only during reperfusion (6). We also assessed the effect of inhibiting XO (by HPLC analysis) with tungsten (7)(8)(9) or allopurinol (10) on ventricular function after ischemia and reperfusion. In addition, we measured H202-dependent aminotriazole inactivation of myocardial catalase activity as an indicator of myocardial H202 production (1 1,12 (13).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts.

Brown¹,

Terada²,

Grosso³

et al. 1988

J. Clin. Invest.

128

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Three lines of investigation indicated that hydrogen peroxide (H202) from xanthine oxidase (XO) contributes to cardiac dysfunction during reperfusion after ischemia. First, addition of dimethylthiourea (DMTU), a highly permeant 02 metabolite scavenger (but not urea) simultaneously with reperfusion improved recovery of ventricular function as assessed by ventricular developed pressure (DP), contractility (+dP/dt), and relaxation rate (-dP/dt) in isolated Krebs-Henseleit-perfused rat hearts subjected to global normothermic ischemia. Second, hearts from rats fed tungsten or treated with allopurinol had negligible XO activities (< 0.5 mU/g wet myocardium compared with > 6.0 mU/g in control hearts) and increased ventricular function after ischemia and reperfusion. Third, myocardial H202-dependent inactivation of catalase occurred after reperfusion following ischemia, but not after ischemia without reperfusion or perfusion without ischemia. In contrast, myocardial catalase did not decrease during reperfusion of ischemic hearts treated with DMTU, tungsten, or allopurinol.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts.

Brown¹,

Terada²,

Grosso³

et al. 1988

J. Clin. Invest.

128

View full text Add to dashboard Cite

show abstract

“…Several techniques have been described for recovery and purification of streptokinase from wild type streptococcus and recombinant streptokinase expressing in host E. coli. De Renzo et al [19] reported highly purified preparations of streptokinase with the use of commercially available streptokinase preparations as the starting material. They reported a specific activity of 90,000-100,000 IU/mg of SK protein, after chromatography of streptokinase preparation twice on DEAE-cellulose [19].…”

Section: Ion-exchange Chromatographymentioning

confidence: 99%

“…The SK gene was then cloned in several Gram-negative and Gram-positive bacteria [13][14][15][16][17]. Several methods of recovery and purification of SK have been described previously which includes purification of wild strain as well as recombinant SK [15,16,[19][20][21][22]. The recombinant target protein in general represents the major fraction of the inclusion body.…”

Section: Introductionmentioning

confidence: 99%

Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli

Babu

Srinivas

Mohan

et al. 2008

Journal of Chromatography B

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“…Molybdenum is essential for mammals (Anke et al, 1977;Pane, 1977;Johnson et al, 1980) but little is known about the physiological role of this metal except the fact that it acts as an active center for several molybdoenzymes such as xanthine dehydrogenase, aldehyde oxidase, and sulfite oxidase (De Renzo et al, 1953;Rajagopalan et al, 1962;Cohen and Fridovitch, 1971) and as a copper antagonist in the ruminant (Furguson et al, 1943). Molybdenum, however reduces the ability of rats to respond to temperature stress through unknown mechanism (Winston et al, 1973) Recently, we found that pretreatment of rats with Na2MoO4 protected them against the acute toxicity of CdC12 as well as against that of I-IgC12 (Yamane and Koizumi, 1982;Yamane et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Protective mechanism of sodium molybdate against the acute toxicity of cadmium in rats. II. Prevention of cytoplasmic acidification

et al. 1991

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In order to clarify the protective mechanism of sodium molybdate against the acute toxicity of cadmium chloride in rat, the effect of in vivo sodium molybdate pretreatment on the cytotoxic action of cadmium in isolated hepatocytes was studied. The cytosolic pH of hepatocytes isolated from untreated rats immediately decreased with incubation in either neutral Hank's balanced salt solution (HBS), pH 7.4, containing 5 microM cadmium chloride minimum or acidic HBS (pH 7.1, 6.8, 6.5, and 6.2). The presence of 5 microM cadmium in HBS adjusted to pH 7.1 aggravated cytosolic acidification induced by the acidic medium alone. Cell viability of hepatocytes incubated in HBS at pH 6.2 was significantly reduced as compared to that of control cells in HBS at pH 7.4, but the presence of cadmium in the acidic HBS had no aggravating action against such a toxic action of the acidic medium although cellular uptake of the metal in the medium increased, as compared to that in HBS at pH 7.4. Molybdenum pretreatment alleviated cytoplasmic acidification induced by the treatment with HBS at pH 7.4 or 7.1 containing cadmium or by extracellular acid load without cadmium. This pretreatment also prevented the loss of cell viability induced by the treatment with HBS at pH 6.2 but could not attenuate that when cadmium was present in the medium. These facts suggest that molybdenum pretreatment alleviated the acute toxicity of cadmium in rat by preventing cytoplasmic acidification caused by the harmful metal.

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The Nature of the Xanthine Oxidase Factor

Cited by 64 publications

References 3 publications

Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts.

Xanthine oxidase produces hydrogen peroxide which contributes to reperfusion injury of ischemic, isolated, perfused rat hearts.

Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli

Protective mechanism of sodium molybdate against the acute toxicity of cadmium in rats. II. Prevention of cytoplasmic acidification

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