Xanthine oxidase-mediated oxidation of epinephrine

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Abstract

It has been reported [M. Oka, J. pharm. Soc. Japan 57, 566 (1961)] that epinephrine is capable of stimulating the oxidation of purines by xanthine oxidase (X.O.). The present investigation shows that such “stimulation” is, in fact, attributable to concomitant oxidation of epinephrine as well as of the purine substrate (hypoxanthine) by X.O. preparations.X.O. does not oxidize epinephrine under the conditions employed in the absence of an oxidizable substrate such as hypoxanthine. The oxidation of epinephrine, in the presence of X.O. and hypoxanthine is inhibited strongly by allopurinol [4-hydroxypyrazolo-(3,4-d)pyrimidine]. Spectroscopic and Chromatographic studies indicate that the product of epinephrine oxidation in the X.O. system is adrenochrome (2,3-dihydro-3-hydroxy-N-methylindole-5,6-quinone). Oxidation of 2-amino-pteridine, 4-aminopteridine and 4-hydroxypteridine by X.O. also induced epinephrine oxidation. In the presence of 4-amino-6,7-dimethylpteridine and 2-amino-4-methyl-pteridine, which are not effective substrates for X.O., appreciable oxidation of epinephrine was not observed.

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    A preliminary account of this work was presented at the meeting of the Federation of American Societies for Experimental Biology, Atlantic City, N.J., April, 1969 [Fedn Proc. 28, 545 (1969)].

    Taken from a portion of a dissertation to be submitted by D.M. Valerino to the Graduate College of The University of Vermont in partial fulfilment of the requirement for the Ph.D. degree.

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