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RISS 인기검색어
- 검색키워드
- 저자 : 이근배 ( Yun Soon Choi (검색결과 2 건)
- 무료
- 기관 내 무료
- 유료
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최연순,이희성,이근배,Choi, Yun-Soon,Lee, Hi-Sung,Lee, Keun-Bai 생화학분자생물학회 1973 한국생화학회지 Vol.6 No.3
발아하는 대두 자엽의 homogenate를 만들어 그 $20,000{\times}g$ 상충액에서 glyoxyl 산 환원 효소(glycollate-NAD oxidoreductase 1. 1. 1. 26)를 조제하여 다시 황산암모늄으로 염석, Sephadex G-200 gel 여과법 및 DEAE-cellulose chromatography에 의하여 정제하였다. Sephadex G-1000 gel 여과법으로 분자량을 측정한 결과 약 158.000의 값을 얻었다. 정제한 이 효소를 1% sodium dodecyl sulfate, $\beta$-mercaptoethanol이 들어 있는 Tris-buffer (pH 7.1)에 넣고 $37^{\circ}$에서 30분간 처리하면 이 효소의 4분의 1의 분자량을 가진 subunit가 생성한다. Polyacrylamide disc gel electrophoresis에 의하여 분자량을 결정하였으며, 그 값은 $41,500{\pm}4,000$이었다. 이 subunit의 amino 산 조성을 분석하였으며 계속하여 몇몇 이화학적 성상을 추구하고 있다. Glyoxylate reductase (glycollate-NAD oxidoreductase, 1. 1. 1. 26) has been prepared from $20,000\;{\times}\;g$ supernatant fraction of homogenate of germinating soy bean seed cotyledons and purified by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-cellulose chromatography. The molecular weight of the enzyme was estimated to be about 158.000 by Sephadex G-100 gel filtration. The purified enzyme has been dissociated into a molecule one fourth the molecular weight of the native enzyme by treatment with 1 per cent sodium dodecyl sulfate, $\beta$-mercaptoethanol and Tris-buffer at pH 7.1 for 30 min. The molecular weight of the subunit was estimated to be approximately $41,500{\pm}4,000$ by polyacrylamide gel electrophoresis. Amino acid composition of the above enzyme molecule are also presented. Some molecular properties of the subunit are being investigated.
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최연순,이희성,이근배 ( Yun Soon Choi,Hi Sung Lee,Keun Bai Lee ) 생화학분자생물학회 1973 BMB Reports Vol.6 No.3
Glyoxylate reductase (glycollate-NAD oxidoreductase, 1. 1. 1. 26) has been prepared from 20,000 x g supernatant fraction of homogenate of germinating soy bean seed cotyledons and purified by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-cellulose chromatography. The molecular weight of the enzyme was estimated to be about 158,000 by Sephadex G-100 gel filtration. The purified enzyme has been dissociated into a molecule one fourth the molecular weight of the native enzyme by treatment with 1 per cent sodium dodecyl sulfate, β-mercaptoethanol and Tris-buffer at pH 7.1 for 30 min. The molecular weight of the subunit was estimated to be approximately 41,500±4,000 by polyacrylamide gel electrophoresis. Amino acid composition of the above enzyme molecule are also presented. Some molecular properties of the subunit are being investigated.
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