Purification and Characterization of Arginine Decarboxylase from Soybean (Glycine max) Hypocotyls |
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Authors: | Nam Kyoung Hee; Lee Sun Hi; Lee JooHun |
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Institution: | Department of Biology, Yonsei University Seoul, Korea 120-749 |
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Abstract: | Arginine decarboxylase (EC 4.1.1.19
EC]
) was purified from soybean,Glycine max, hypocotyls by a procedure which includes ammoniumsulfate fractionation, acetone precipitation, gel filtrationchromatography, and affinity chromatography. Using this procedure,ADC was purified to one band in non-denaturing PAGE. The purifiedADC has an Mr of 240 kDa based on gel filtration chromatographyand is a trimer of identical subunits which has an estimatedMr of 74 kDa based on SDS-PAGE. ADC is active between 30 and50°C and has a Km value of 46.1 µM. ADC is very sensitiveto agmatine or putrescine but not to spermidine or spermine.In the presence of 0.5 mM agmatine (or putrescine), the enzymeactivity was inhibited by 70%. However, at the same concentrationof spermidine (or spermine), the enzyme activity was inhibitedby only 1020%. (Received April 2, 1997; Accepted August 18, 1997) |
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