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한국환경생물학회 / v.21, no.1, 2003년, pp.60-65 
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( The Enzymatic Characteristics of the Cytidine Deaminase in Salmonella typhimurium ) |
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| 초 록 |
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| The cytidine deaminase was partialy purified with sephadex G-200 and the characteristics of the enzyme were clarified. The molecular mass of the plasmid-encoded protein was identified as about 30 kDa in a minicell system. The native enzyme was estimated to have the molecular mass of 60 kDa by gel filtration. This indicates that the native enzyme may exist as a dimer composed of two identical subunits. The enzyme was reasonably stable in the pH range of 6 to 9, and was labile under high temperature above $50^{circ}C$. Mercaptoethanol, pCMB, mercury and copper were found to inhibit the enzyme activity. The cytidine analogues of bromo- and iodo-(deoxy)-cytidine were also found to inhibit the activity, while fluorodeoxycytidine and azacytidine were found to activate it. Deoxycytidine, cytidine, ara-C and Methyldeoxycytidine have excellent substrates for the enzyme. |
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| 키워드 |
| cytidine deaminase;Salmonella typhimurium;inhibitor;molecular weight; |
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환경생물 / v.21, no.1, 2003년, pp.60-65
한국환경생물학회
ISSN : 1226-9999
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200311921575213)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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