Purification and Characterization of Arginine Decarboxylase from Soybean (Glycine max) Hypocotyls
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概要
- 論文の詳細を見る
Arginine decarboxylase (EC 4.1.1.19) was purified from soybean, Glycine max, hypocotyls by a procedure which includes ammonium sulfate fractionation, acetone precipitation, gel filtration chromatography, and affinity chromatography. Using this procedure, ADC was purified to one band in non-denaturing PAGE. The purified ADC has an M, of 240 kDa based on gel filtration chrolnatography and is a trimer of identical subunits which has an estimated M* of 74 kDa based on SDS-PAGE. ADC is active between 30 and 50℃ and has a K~ value of 46.1 μM. ADC is very sensitive to agmatine or putrescine but not to spermidine or spermine. In the presence of 0.5 nlM agmatine (or putrescine), the enzylne activity was inhibited by 70010. However, at the same concentration of spermidine (or spermine), the enzyme activity was inhibited by only 10-20%.
- 日本植物生理学会の論文
著者
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LEE Joo
Departments of Surgery, Seoul National University College of Medicine
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LEE Sun
Department of Nuclear Engineering, Chosun University
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Lee S
Yonsei Univ. Seoul Kor
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Lee J
Kookmin Univ. Seoul Kor
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Nam Kyoung
Department of Biology, Yonsei University
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Nam K
Univ. Michigan Mi Usa
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Lee Joo
Department Of Biology Yonsei University
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Lee Sun
Department Of Biotechnology Yonsei University
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Nam Kyoung
Department Of Biological Science Sookmyung Women's University
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Lee Sun
Department Of Biological Scienceand Basic Science Research Institute Sungkyunkwan University
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Lee JooHun
Department of Biology, Yonsei University
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