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KMID : 0377619670120050499
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Korean Jungang Medical Journal
1967 Volume.12 No. 5 p.499 ~ p.506
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Partial Purification and Isoaymic Nature of Guanine Deaminase from Rat Liver
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Kim, Sung-Wun/金昇元
Lee, Ho-Min/Kim, In-Suk/李鎬敏/金仁淑
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Abstract
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Purine catabolism involves interconversions between purines at the level of the mono phosphates, the ribosides, and the free bases. It gives rise to uric acid as the end product in man and other primates, as well as in birds and terrestial reptiles, however in mammals other than the primates, allantoin is the chief end product.
The authors are interested in the mode of a certain enzymatic regulatory mechanism which might exert its effect over this complex interconversion phenomena among the purine family, and intended to study the enzyme which converts guanine into xanthine as a prelim at thee level of the free bases, adenine appears to lack a deammase in the animal body while guanine is deammated to xanthine. (1,2)
The author noticed however that the reports on the partial purification and properties of the guanine deaminase are rare except for a few clinical studies,(3-6), and therefore tried to look for a suitable method in the present paper to meet our purpose.
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