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RISS 인기검색어
- 검색키워드
- 저자 : 박성희 ( Keun Bai Lee (검색결과 2 건)
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이근배,채영복,박성희,Lee, Keun-Bai,Chae, Yung-Bog,Park, Sung-Hee 생화학분자생물학회 1969 한국생화학회지 Vol.2 No.2
발아하는 대두 자엽에서 glyco1ic acid oxidase (glycolate: $O_2$ oxidoreductase, EC 1.1.3.1)를 여러 과정을 거쳐 약 680배 정제하였다. 정제된 효소의 최적 pH 는 8.0 이다. 이 효소의 cofactor 는 flavin mononucleotide 이다. glycolic acid 에 대한 Michaelis constant 는 $1.4{\times}10^{-4}M$ 이다. KCN 의 첨가는 이 효소의 활성을 약 4 배 증가시켰으며 p-chloromercuribenzoate 및 iodoacetate 는 저해작용을 나타냈다. Sephadex gel filtration 에 의하여 측정한 분자량은 약 68,000 이다. A 680-fold purifcation of glycolate oxidase (glycolate: $O_2$ oxidoreductase. EC 1.1.3.1) has been achieved from $20,000{\times}g$ supernatant fraction of germinating Soy bean seed embryos by means of ammonium sulfate precipitation. acid precipitation, Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The pH optimum for the reaction is 8.0 and apparent Michaelis constant was estimated as $1.0{\times}10^{-4}M$ for glycolic acid. Disc electrophoresis on acrylamide gel was carried out at various purification steps of the enzyme, and the final preparation was found to consist of one protein component. The molecular weight of the enzyme was estimated to be approximately 68,000 by Sephadex G-100 gel filtration. FMN and FAD were found to be efficient cofactors, FMN being more favorable than FAD. The enzyme was activated by KCN and inhibited by p-chloromercuribenzoate and iodoacetate.
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이근배,채영복,박성희 ( Keun Bai Lee,Young Bok Chae,Sung He Park ) 생화학분자생물학회 1969 BMB Reports Vol.2 No.2
A 680-fold purifcation of glycolate oxidase (glycolate : 02 oxidoreductase. EC 1. 1. 3. 1) has been achieved from 20,000 × g supernatant fraction of germinating Soy bean seed embryos by means of ammonium sulfate precipitation. acid precipitation, Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The pH optimum for the reaction is 8.0 and apparent Michaelis constant was estimated as 1.0 × 10^(-4) M for glycolic acid. Disc electrophoresis on acrylamide gel was carried out at various purification steps of the enzyme, and the final preparation was found to consist of one protein component. The molecular weight of the enzyme was estimated to be approximately 68,000 by Sephadex G-100 gel filtration. FMN and FAD were found to be efficient cofactors, FMN being more favorable than FAD. The enzyme was activated by KCN and inhibited by p-chloromercuribenzoate and iodoacetate,
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