IN VITRO STUDY OF 6-MERCAPTOPURINE OXIDATION BY MOLYBDENUM HYDROXYLASES

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RASHIDI MOHAMMAD REZA

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Journal: PHARMACEUTICAL SCIENCES Year:2000 | Volume:- | Issue:3 Page(s): 33-42

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Title

IN VITRO STUDY OF 6-MERCAPTOPURINE OXIDATION BY MOLYBDENUM HYDROXYLASES

Author(s)

RASHIDI MOHAMMAD REZA | Issue Writer Certificate

Keywords

MERCAPTOPURINEQ3

MOLYBDENUM HYDROXYLASEQ3

ALDEHYDE OXIDASEQ3

XANTHINE OXIDASEQ2

Abstract

In spite of over 40 years of 6-MERCAPTOPURINE application, many aspects of complex pharmacology and metabolism of this drug remain unclear. It is thought that 6- MERCAPTOPURINE is oxidized to the inactive metabolite, 6-thiouric acid through 6-thioxanthine or 8-oxo-6-MERCAPTOPURINE in its catabolic metabolic pathways. Although this oxidative deactivation of 6-MERCAPTOPURINE has been attributed to the action of one of two MOLYBDENUM HYDROXYLASEs, XANTHINE OXIDASE, the role of other MOLYBDENUM HYDROXYLASE, ALDEHYDE OXIDASE, in the oxidation of 6-MERCAPTOPURINE has not been investigated in more details. In the present study, the role of aldehyde oxi'dase and XANTHINE OXIDASE in the oxidation of 6-MERCAPTOPURINE has been investigated. 6-MERCAPTOPURINE was incubated with bovine milk XANTHINE OXIDASE or partially purified guinea pig liver MOLYBDENUM HYDROXYLASE fractions and the reactions were monitored by spectrophotometric and HPLC methods in the absence and presence of XANTHINE OXIDASE inhibitor, allopurinol, and some ALDEHYDE OXIDASE inhibitors. XANTHINE OXIDASE-catalyzed oxidation of 6-MERCAPTOPURINE was completely inhibited by allopurinol with ALDEHYDE OXIDASE inhibitors having no significant inhibitory effects. With guinea pig liver fractions, however, the initial oxidation rate of 6-MERCAPTOPURINE was inhibited by 39-66% in the presence of allopurinol and ALDEHYDE OXIDASE inhibitor. The HPLC analysis of the reaction was indicative of oxidative conversion of 6-MERCAPTOPURINE to 6-thiouric acid through 6-thioxanthine. The oxidation of 6- MERCAPTOPURINE was inhibited by >90% and 45-49% in the presence of allopurinol and ALDEHYDE OXIDASE inhibitors, respectively. Based on the results obtained, it may be suggested that 6-MERCAPTOPURINE is oxidized by both MOLYBDENUM HYDROXYLASEs to 6-thiouric acid through 6-thioxanthine. The first reaction which is the rate limiting step is catalyzed by XANTHINE OXIDASE, whereas the second reaction is catalyzed by both MOLYBDENUM HYDROXYLASEs.

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APA: Copy

RASHIDI, MOHAMMAD REZA. (2000). IN VITRO STUDY OF 6-MERCAPTOPURINE OXIDATION BY MOLYBDENUM HYDROXYLASES. PHARMACEUTICAL SCIENCES, -(3), 33-42. SID. https://sid.ir/paper/48516/en

Vancouver: Copy

RASHIDI MOHAMMAD REZA. IN VITRO STUDY OF 6-MERCAPTOPURINE OXIDATION BY MOLYBDENUM HYDROXYLASES. PHARMACEUTICAL SCIENCES[Internet]. 2000;-(3):33-42. Available from: https://sid.ir/paper/48516/en

IEEE: Copy

MOHAMMAD REZA RASHIDI, “IN VITRO STUDY OF 6-MERCAPTOPURINE OXIDATION BY MOLYBDENUM HYDROXYLASES,” PHARMACEUTICAL SCIENCES, vol. -, no. 3, pp. 33–42, 2000, [Online]. Available: https://sid.ir/paper/48516/en

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