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Ksantin dehidrogenaza (Serbian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Ksantin dehidrogenaza" in Serbian language version.

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15nih.gov
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3archive.org
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archive.org

nih.gov

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  • Battelli, M.G. & Lorenzoni, E. (1982). „Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver”. Biochem. J. 207: 133—138. PMID 6960894. 
  • Della Corte, E. & Stirpe, F. (1972). „The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme”. Biochem. J. 126: 739—745. PMID 4342395. 
  • Parzen, S.D. & Fox, A.S. (1964). „Purification of xanthine dehydrogenase from Drosophila melanogaster”. Biochim. Biophys. Acta. 92: 465—471. PMID 14264879. 
  • Rajagopalan, K.V. & Handler, P. (1967). „Purification and properties of chicken liver xanthine dehydrogenase”. J. Biol. Chem. 242: 4097—4107. PMID 4294045. 
  • Smith, S.T., Rajagopalan, K.V. and Handler, P. (1967). „Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus”. J. Biol. Chem. 242: 4108—4117. PMID 6061702. 
  • Ikegami, T. & Nishino, T. (1986). „The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver”. Arch. Biochem. Biophys. 247: 254—260. PMID 3459393. 
  • Engerson, T.D., McKelvey, T.G., Rhyne, D.B., Boggio, E.B., Snyder, S.J. and Jones, H.P. (1987). „Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues”. J. Clin. Invest. 79: 1564—1570. PMID 3294898. 
  • Saito, T., Nishino, T. and Tsushima, K. (1989). „Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them”. Adv. Exp. Med. Biol. 253B: 179—183. PMID 2610112. 
  • Parschat, K., Canne, C., Hüttermann, J., Kappl, R. and Fetzner, S. (2001). „Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization”. Biochim. Biophys. Acta. 1544: 151—165. PMID 11341925. 
  • Ichida, K., Amaya, Y., Noda, K., Minoshima, S., Hosoya, T., Sakai, O., Shimizu, N. and Nishino, T. (1993). „Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene”. Gene. 133: 279—284. PMID 8224915. 
  • Enroth, C., Eger, B.T., Okamoto, K., Nishino, T., Nishino, T. and Pai, E.F. (2000). „Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. USA. 97: 10723—10728. PMID 11005854. 
  • Truglio, J.J., Theis, K., Leimkuhler, S., Rappa, R., Rajagopalan, K.V. and Kisker, C. (2002). „Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus”. Structure. 10: 115—125. PMID 11796116. 
  • Hille, R. (1996). „The mononuclear molybdenum enzymes”. Chem. Rev. 96: 2757—2816. PMID 11848841. 
  • Taibi, G., Di Gaudio, F. and Nicotra, C.M. (2008). „Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells”. J. Enzyme Inhib. Med. Chem. 23: 317—327. PMID 18569334. 
  • Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F. and Nishino, T. (2008). „Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase”. FEBS J. 275: 3278—3289. PMID 18513323.