Purification and properties of phenylalanine ammonia-lyase from Chinese cabbage

  • Lim, Hye-won
  • Sa, Jae-hoon
  • Kim, Tae-soo
  • Park, Eun-hee
  • Park, Soo-sun
  • 외 1명
Citations

SCOPUS

5

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 45°C, respectively. Its activity is greatly inhibited by Zn2+ ion, and strongly activated by caffeic acid. The purified PAL has some different characteristics compared to those obtained with other PALs.

키워드

CharacterizationChinese cabbage (Brassica campestris ssp. napus var. pekinensis)Phenylalanine ammonia-lyasePurification
제목
Purification and properties of phenylalanine ammonia-lyase from Chinese cabbage
저자
Lim, Hye-wonSa, Jae-hoonKim, Tae-sooPark, Eun-heePark, Soo-sunLim, Chang-jin
발행일
1998
유형
Article
저널명
Journal of Biochemistry and Molecular Biology
31
1
페이지
31 ~ 36