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KMID : 0364219740170030107
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Korean Journal of Zoology
1974 Volume.17 No. 3 p.107 ~ p.116
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Metabolism of Pyrimidine Deoxyribonucleosides and Heat-resistivity of CdR-aminohydrolase in the Mouse Small Intestine
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Kang Man-Sik
Rhee Juong-Gile
Cho Joong-Myung
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Abstract
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The metabolism of CdR-2-$^14 C$ and UdR-2-$^14 C$ in mouse small intestine has been studied in connection with the effect of heat treatment on the enzymes concerned in vitro. CdR-2-$^14 C$ is deaminated reaidly by CdR-aminohydrolase at nucleoside level and then degraded into U by the action of nucleosidase which is quite resistant to cleave N-pentose bond of cytosine nucleosides, CdR and CR. High inactivation temperature of $80^\\circC$ was observed for CdR-aminohydrolase, while nucleosidase has an inactivation temperature of $60^\\circC$. CdR-aminohydrolases in various tissues of mouse were inactivated at $80^\\circC$, but not one in tissues of rabbit. It might be assumed that there are correlations between order specificity and inactivation temperature of the enzyme. A physiological significance of the appearance of CdR-aminohydrolase in differentiated tissues of mammals possibly be regarded as a main function in catabolic pathways.
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