Please use this identifier to cite or link to this item:
10.1046/j.1432-1327.1998.2570178.x
Title: | Identification of an N-hydroxyguanidine reducing activity of xanthine oxidase |
Authors: | Dambrova, Maija Uhlén, Staffan Welch, Christopher J. Wikberg, Jarl E.S. |
Keywords: | Guanoxabenz;N-hydroxyguanidine;Reduction;Xanthine oxidase;1.4 Chemical sciences;1.6 Biological sciences;3.1 Basic medicine;1.1. Scientific article indexed in Web of Science and/or Scopus database;Biochemistry |
Issue Date: | 1-Oct-1998 |
Citation: | Dambrova , M , Uhlén , S , Welch , C J & Wikberg , J E S 1998 , ' Identification of an N-hydroxyguanidine reducing activity of xanthine oxidase ' , European Journal of Biochemistry , vol. 257 , no. 1 , pp. 178-184 . https://doi.org/10.1046/j.1432-1327.1998.2570178.x |
Abstract: | A guanoxabenz [1-(2,6-dichlorobenzylideneamino)-3-hydroxyguanidine; an N-hydroxyguanidine] reducing enzymatic activity of rat spleen cytosol was investigated by means of protein purification and N-terminal amino acid sequencing, the reducing activity was shown to reside in xanthine oxidase. The action of the enzyme on guanoxabenz resulted in the formation of guanabenz [1-(2,6-dichlorobenzylideneamino) -3-guanidine]; the product formation could be monitored by HPLC and its identity was confirmed by NMR analysis. The reduction of guanoxabenz required xanthine or NADH as reducing substrates, while the process could be blocked by allopurinol, a selective inhibitor of xanthine oxidase. By using bovine milk xanthine oxidase, the guanoxabenz reducing activity of the enzyme was also verified. We conclude that guanoxabenz is a novel electron acceptor structure for xanthine oxidase. |
DOI: | 10.1046/j.1432-1327.1998.2570178.x |
ISSN: | 0014-2956 |
Appears in Collections: | Research outputs from Pure / Zinātniskās darbības rezultāti no ZDIS Pure |
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Identification_of_an_N_hydroxyguanidine.pdf | 202.05 kB | Adobe PDF | View/Open |
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