Applied Biological Chemistry
- Volume 30 Issue 3
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- Pages.219-226
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- 1987
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- 2468-0834(pISSN)
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- 2468-0842(eISSN)
Purification and Characterization of Peroxidase Isozyme C from Mung Bean
녹두의 Peroxidase Isozyme C의 생화학적 성장
- Lee, Sang-Kap (Department of Agricultural Chemistry, College of Agriculture, Kyungpook National University) ;
- Park, Woo-Churl (Department of Agricultural Chemistry, College of Agriculture, Kyungpook National University)
- Published : 1987.09.30
Abstract
Peroxidase isozyme C was isolated from mung bean cotyledon and purified to homogeneity as ascertained by chromatography and polyacrylamide gel electrophoresis, and then crystallized. Purification procedures included ammonium sulfate precipitation and column chromatography on Sephadex G-75, DEAE-cellulose and DEAE-Sephadex A-50. Peroxidase isozyme C was purified about 63 fold with 5% recovery. Isozyme C showed optimal activity at pH 5.0 with o-dianisidine and at pH 6.0 with guaiacol as substrate, and the optimal temperature was
녹두의 자엽에서 peroxidase isozyme을
Keywords