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KMID : 0578319970070060715
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Molecules and Cells
1997 Volume.7 No. 6 p.715 ~ p.720
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Purification and properties of Phenulalanine Ammonia-Lyase from Leaf Mustard
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Lim, Hye-won
Park, soo-Sun/Lim, Chang-Jin
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Abstract
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Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5), the first enzyme in phenylpropanoid biosynthesis, catalyzes the elimination of ammonium ion from L-phenylalanine. In the present study, PAL was purified through ammonium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 chromatography, and Q-Sepharose chromatography from the cytosolic fraction of leaf mustard (Brassica juncea var. integrifolia). It consists of 4 subunits, each having an estimated molecular weight of about 40,000 on SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal pH and temperature of the purified enzyme are 9.0 and 45 ℃, respectively. Its activity is inhibited by Zn^(2+) ion, and it is strongly activated by caffeic acid. The purified PAL seems to have some characteristics different from those obtained with other PALs.
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