미생물학회지 (Korean Journal of Microbiology)
- 제32권4호
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- Pages.315-321
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- 1994
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- 0440-2413(pISSN)
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- 2383-9902(eISSN)
Pleurotus ostreatus에서 분리된 Glyoxalase I의 특성
Purification and Characterization of Glyoxalase I from Pleurotus ostreatus
- 김성태 (서울대학교 자연과학대학 미생물학과, 분자미생물학연구센터) ;
- 양갑석 (서울대학교 자연과학대학 미생물학과, 분자미생물학연구센터) ;
- 석영재 (서울대학교 자연과학대학 미생물학과, 분자미생물학연구센터) ;
- 허원기 (서울대학교 자연과학대학 미생물학과, 분자미생물학연구센터) ;
- 강사욱 (서울대학교 자연과학대학 미생물학과, 분자미생물학연구센터)
- Kim, Seong-Tae (Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
- Yang, Kap-Seok (Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
- Seok, Yeong-Jae (Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
- Huh, Won-Ki (Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University) ;
- Kang, Sa-Ouk (Department of Microbiology, College of Natural Sciences, and Research Center for Molecular Microbiology, Seoul National University)
- 발행 : 1994.01.01
초록
Pleurotus ostreatus로부터 glyoxalase I(S-lactoyl-glutathione methylglyoxal lyase, EC 4.4.1.5)이 S-hexylglutathione affinity chromatography, Sephadex G-150 gel permeation chromatography, DEA-sepharose A-50 CL-6B ion exchange chromatography를 통해 순수 분리되었다. 이 결과, 전체 활성도의 21.7% fmf 수확하였으며, 분리 배수는 2,294 배 이었다. Gel filtration chromatography로 측정한 효소의 분자량은 34 kDa이며, SDS-PAGE 결과 본 효소는 분자량 17 kDa인 동일한 소단위체 두 개로 구성된 이합체라고 생각된다. Methylglyoxal과 phenylglyoxal에 대한
Glyoxalase I was purified 2,294-fold from Pleurotus ostreatus by S-hexylglutathione affinity chromatography, Sephadex G-150 gel filtration chromatography and DEAE-sepharose A-50 CL-6B ion exchange chromatography with an overall yield of 21.7%. The molecular mass determined by gel filtration was found to be approx. 34 kDa. SDS-PAGE revealed that the enzyme consists of two identical subunits with a molecular mass of approx. 17 kDa. The K sub(m) values of this enzyme for methylglyoxal and phenylglyoxal were 0.39 mM and 0.22 mM, respectively. And this enzyme had a strong affinity for L-xylosone and hydroxypyruvaldehyde. The enzyme showed its optimal activity at pH 6.5-7.5 and at
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