Bovine milk xanthine oxidase

Boroxazothienopyridines, 4, 1029-1032 Borsche synthesis, 3, 44 Botrydiplodin mass spectrometry, 4, 585 Boulton-Katritzky rearrangement, 5, 288 Bovine milk xanthine oxidase substrates, 1, 234 Bradsher reaction... 

Panoutsopoulos GI, Beedham C. Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes. Acta Biochim Pol 2004 51(3) 649-663. 

In 1975, the Life Sciences Research Office of the Federation of American Societies for Experimental Biology (Carr et al. 1975), upon an extensive review of the available evidence, concluded that it was doubtful whether XO in homogenized cow s milk was a causal or risk factor for heart disease. More recently, Clifford et al (1983) and Deeth (1983), in critical reviews of the homogenized cow s milk XO hypothesis, have arrived at a similar, if not more definitive, conclusion. As stated by Clifford et al. (1983), experimental evidence has failed to substantiate, and in many cases has refuted, the hypothesis that homogenized bovine milk xanthine oxidase intake or plasmalogen depletion are causal factors in the development of atherosclerosis. And, according to Deeth (1983), there appears to be no unequivocal evidence that the absorbed enzyme has any pathological effects that may contribute to development of atherosclerotic heart disease. ... 

Carr, C. J., Talbot, J. M. and Fisher, K. D. 1975. A review of the significance of bovine milk xanthine oxidase in the etiology of atherosclerosis. Life Science Research Office, Federation of American Societies for Experimental Biology, Bethesda, Md. (Prepared for the Food and Drug Administration, Washington, D. C., Contract No. FDA 223-75-2090.)... 

Clifford, A. J., Ho, C. Y. and Swenerton, H. 1983. Homogenized bovine milk xanthine oxidase A critique of the hypothesis relating to plasmalogen depletion and cardiovascular disease. Am J. Clin. Nutr. 38, 327-332. 

Ho, C. Y., Crane, R. T. and Clifford, A. J. 1978. Studies on lymphatic absorption of and the availability of riboflavin from bovine milk xanthine oxidase. J. Nutr. 108, 55-60. 

Rzucidlo, S. J. and Zikakis, J. P. 1979. Correlation of dairy food intake with human antibody to bovine milk xanthine oxidase. Proc. Soc. Exp. Biol Med. 160, 477-482. 

Zikakis, J. P., Rzucidlo, S. J. and Biasotlo, N. O. 1977. Persistence of bovine milk xanthine oxidase activity after gastric digestion in vivo and in vitro. J. Dairy Sci. 60, 533-541. 

Nathans, G. R. and Hade, E. P. K. 1978. Bovine milk xanthine oxidase. Purification by ultrafiltration and conventional methods which omit addition of proteases. Some criteria for homogeneity of native xanthine oxidase. Biochim. Biophys. Acta 526, 328-344. 

Waud, W. R., Brady, F. O., Wiley, R. D. and Rajagopalan, K. V. 1975. A new purification procedure for bovine milk xanthine oxidase Effect of proteolysis on the subunit structure. Arch. Biochem. Biophys. 169, 695-701. 

Although attempts to identify either enzyme in human sera have so far proved unsuccessful, exceptionally high concentrations of antibodies to xanthine oxidase have been found in human sera as well as in that from various animals [124]. Despite these unusually high levels, it is proposed that the antibodies result from self-immunization to the xanthine oxidase antigen present in the endothelial cells of capillaries, although the authors also acknowledge that the antibodies in human sera may be induced by bovine milk xanthine oxidase ingested in dairy products [ 124]. 

Substrate Bovine milk xanthine oxidase Hepatic aldehyde oxidase ... 

Rabbit liver aldehyde oxidase. b Bovine milk xanthine oxidase. c Rat liver aldehyde oxidase. 

Febuxostat (1) inhibits bovine milk xanthine oxidase and mouse and rat liver xanthine oxidase/xanthine dehydrogenase with ICso values of 1.4, 1.8, and 2.0 nM, respectively ICso values obtained for allopurinol (2) for the same substance were 1700, 380, and 1100 nM, respectively. As shown in Table 1, febuxostat is the most potent inhibitor against xanthine oxidase. ... 

A comparison of the substrate specificities of bovine milk xanthine oxidase and rabbit liver aldehyde oxidase revealed both similarities and differences [10]. Both enzymes exhibited a preference for heterocycles which contain a condensed-pyrimidine ring system (Figure 3). Of the unsubstituted ring systems studied,... 

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