BMB Reports
- 제31권1호
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- Pages.31-36
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- 1998
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- 1976-670X(eISSN)
Purification and Properties of Phenylalanine Ammonia-lyase from Chinese Cabbage
- Lim, Hye-Won (Division of Life Sciences, College of Natural Sciences, Kangwon National University) ;
- Sa, Jae-Hoon (Division of Life Sciences, College of Natural Sciences, Kangwon National University) ;
- Kim, Tae-Soo (Division of Life Sciences, College of Natural Sciences, Kangwon National University) ;
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Park, Eun-Hee
(College of Pharmacy, Sookmyung Women's University) ;
- Park, Soo-Sun (College of Pharmacy, Sookmyung Women's University) ;
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Lim, Chang-Jin
(Division of Life Sciences, College of Natural Sciences, Kangwon National University)
- 발행 : 1998.01.31
초록
Phenylalanine ammonia-lyase (PAL; EC 4.3.1.5), the first enzyme in the phenylpropanoid biosynthesis, catalyzes the elimination reaction of ammonium ion from L-phenylalanine. PAL was purified from the cytosolic fraction of Chinese cabbage (Brassica campestris ssp. napus var. pekinensis) through ammonium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 chromatography, and Q-Sepharose chromatography. It consists of four identical subunits, the molecular mass of which was estimated to be about 38,000 daltons on SDS-PAGE. The optimal pH and temperature of the purified enzyme are 8~9 and
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