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Vitreoscilla Catalase 의 분리 및 특성에 관한 연구
박기인,박충웅 ( Kie In Park,Chung Ung Park ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.6
Vitreoscilla is a gram-negative bacterium that contains a unique bacterial hemoglobin and grows very well under the condition of low oxygen concentration. It also contain a bacterial catalase to be not correspond with another species on genus Beggiatoa. The primary function of Vitreoscilla catalase may be to remove hydrogen peroxide produced by ViWb oxidation. The molecular size of the catalase was estimated to be approximately 250,000 Da. The subunit structure of this enzyme may be A₂B₂ (A : MW 64,000 Da, B : MW 58,000 Da) but is not clear in the research reported here. Optimum pH is 7.0∼8.0 for catalase activity and Soret peak on absorption spectra of oxidized catalase is represented in 406 ㎚ and Soret peak of reduced form from sodium dithionite moved at 442 ㎚. Vitreoscilla catalase is unstable a high tempernture, and its Michealis constant, K_m was 0.016 M hydrogen peroxide. The turnover number of the enzyme was 25,000 mol. The 0.25 mM potassium cyanide was competitive inhibitor and the dissociation constant of the enzyme-inhibitor complex was 0.67 mM. N-terminal amino acid sequences of two subunits are determined for the probe synthesis using to the cloning of Vitreoscilla catalase gene.
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Vitreoscilla Hemoglobin 유전자가 재조합 대장균의 성장조건에 미치는 영향
박충웅,박기인 한국유전학회 1994 Genes & Genomics Vol.16 No.4
In this rearch plasmid pMK79 was engineered by pMK57 which contain Bacillus stearothermophilus α-amylase gene into pUC8 and pUC8: 15 which has Vitreoscilla hemoglobin gene (VtHb). Both pMK57 and pMK79 were transformed into Escherichia coli. The presence of Vitreoscilla hemoglobin expressed VtHb improves the growth of MK79 (pMK79 transformant) in an oxygen limited environment compared to strain MK57 (pMK57 trasformant) as using efficiently oxygen. Expression of the amylase gene in both systems was also measured. The result showed that amylase production in MK79 was also significantly higher in mid log and late log phases than in MK57. It was also found that α-amylase gene transcription can occur from the B. stearothermophilus promoter as well, at induced levels, from the lac promoter in pUC8.
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Vitreoscilla Catalase의 분리 및 특성에 관한 연구
박기인,박충웅 全北大學校 基礎科學硏究所 1994 基礎科學 Vol.17 No.-
Vitreoscilla는 헤모글로빈을 갖고 있는 그람 음성 미생물체로써, 이 헤모글로빈을 통한 산소호흡으로부터 파생된 과산화수소를 많은 양의 catalase를 합성하여 효과적으로 분해한다. 이 효소의 분자량은 약 250,000 daltons이며, subunit의 구조는 모든 다른 미생물체에서 보여주는 A_4와는 달리 A_2B_2(A:64,000 daltons, B:58,000 daltons)를 보였다. 최적 pH는 7.0∼8.0이었고, oxidized form의 absorption spectra에서 Soret peak는 406㎚에서 나타났으며 reducing agent인 sodium dithionite로부터 야기된 reduced form의 Soret peak는 442㎚로 이동되었다. 또한 이 효소는 열에 불안정 했고, K_m값은 0.016M hydrogen peroxide를 나타냈으며, tumover number는 25,000mol이었다. 0.25mM potassium cyanide는 경쟁적 저해로써 이 효소의 활성을 저해하였으며, 효소-저해제 복합체의 dissociation constant는 0.67mM을 보였다. 두 subunits의 N-말단 아미노산 서열이 다음 실험을 위한 oligonucleotide 합성을 위하여 결정되었다. Vitreoscilla is a gram-negative bacterium that contains a unique bacterial hemoglobin and grows very well under the condition of low oxygen concentration. It also contain a bacterial catalase to be not correspond with another species on genus Beggiatoa. The primary function of Vitreoscilla catalase may be to remove hydrogen peroxide produced by VitHb oxidation. The molecular size of the catalase was estimated to be approximately 250,000 Da. The subunit structure of this enzyme may be A_2B_2 (A: MW 64,000 Da, B: MW 58,000 Da) but is not clear in the research reported here. Optimum pH is 7.0∼8.0 for catalase activity and Soret peak on absorption spectra of oxidized catalase is represented in 406㎚ and Soret peak of reduced form from sodium dithionite moved at 442㎚. Vitreoscilla catalase is unstable a high temperature, and its Michealis constant, K_m, was 0.016 M hydrogen peroxide. The tumover number of the enzyme was 25,000mol. The 0.25mM potassium cyanide was competitive inhibitor and the dissociation constant of the enzyme-inhibitor complex was 0.67mM. N-terminal amino acid sequences of two subunits are determined for the probe synthesis using to the cloning of Vitreoscilla catalase gene.
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