Journal of Ginseng Research
- Volume 19 Issue 3
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- Pages.237-243
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- 1995
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- 1226-8453(pISSN)
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- 2093-4947(eISSN)
Purification and Characterization of Agmatine Iminohydrolase from Panax ginseng C.A. Meyer(I)
인삼(Panax ginseng C.A. Meyer) Agmatine Iminohydrolase의 정제 및 특성(I)
- Kim, Hyo-Sup (Department of Biochemistry, College of Science, Yonsei University) ;
- Kim, Hee-Jung (Department of Biochemistry, College of Science, Yonsei University) ;
- Cho, Young-Dong (Bioproduct Research Center)
- Published : 1995.12.01
Abstract
Agmatine iminohydrolase (EC 3.5.3.12) catalyzes the hydrolysis of agmatine into putrescine. The enzyme seems to be one of the critical enzymes in putrescine biosynthesis. The enzyme was purified to homogeneity from Panax ginseng C.A. Meyer by combined method of ammonium sulfate 1 fractionation, DEAR anion exchange column, hydroxyapatite column and agmatine carboxyhexyl Sepharose 4B affinity column. The molecular weight estimated by native pore gadient polyacrylamide gel electrophoresis was 71, 000 Dalton, while that estimated by SDS-PAGE was 70, 000 Dalton, indicating a monomeric enzyme. The optimal pH and temperature were 9.0 and 37