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Partial Purification of Nuclease $P_1$ from Penicillium citrinum by Tannin Adsorption Chromatography
서원철,임번산,전문진,엠 써네쓰,Suh, W.C.,Lim, B.S.,Chun, M.,Sernetz, M. Korean Society for Biochemistry and Molecular Biol 1987 한국생화학회지 Vol.20 No.1
효소 단백질에 대한 탄닌의 특이적 흡착성질과 흡착 크로마토그래피의 응용성에 대하여 검토하였다. 고정화 탄닌 1 g당 nuclease $P_1$의 흡착량은 40 mg 이었으며, 흡착된 nuclease $P_1$을 90%의 높은 수율로 회수할수 있었다. 황산 암모니움 염석과 단백질 정제의 새로운 시도방법으로서 탄닌 흡착 크로마토그래피에 의하여 nuclease $P_1$의 부분정제를 시도한 결과 nuclease $P_1$의 비활성은 15.6 배 향상되었으며, 이때 수율은 55.3% 였다. As a new approach for protein purification, affinity characteristics of tannin for enzyme protein and its applicability to adsorption chromatography were investigated. Crude nuclease $P_1$ was first purified by fractionation of ammonium sulfate followed by tannin adsorption chromatography. Result showed that adsorption capacity of nuclease $P_1$ onto one gram of immobilized tannin was 40 mg and recovery yield of the enzyme was 90%. Specific activity of the purified nuclease $P_1$ increased to 15.6 fold higher than that of crude extract, recovering 55.3% of enzyme yield.
서원철,임번삼,전문진,엠 써네쓰,Suh, W.C.,Lim, B.S.,Chun, M.,Sernetz, M. Korean Society for Biochemistry and Molecular Biol 1987 한국생화학회지 Vol.20 No.1
Penicillum citrinum 의 nuclease $P_1$을 탄닌 및 p-benzoquinone을 사용하여 셀룰로오스에 고정화하였다. 고정화 nuclease P1의 최적 반응온도는 $70^{\circ}C$로서 수용성 효소와 별 차이가 없었으며 최적pH는 5.5에서 5.0으로 산성쪽으로 약간 이동하였다. 또한 기질인 RNA에 대해 수용성 효소와 고정화 효소의 Km값은 각각 0.92% 및 1. 48%로 나타났다. 최종적으로 Packed-Bed Reactor와 Continuous-Flow Stirred-Tank Reactor에 의한 5'- 누클레오티드의 연속적 생산을 각각 비교 검토하여 보았다. Nuclease $P_1$ from Penicillium citrinum was immobilized on cellulose by covalent binding method. Their general properties and applicational possibilities were investigated. Optimum reaction temperature of immobilized nuclease $P_1$ was $70^{\circ}C$ with broader activity range than that of native enzyme, while optimum pH was shifted to pH 5.0 from pH 5.5 for the native enzyme. Km values of native and immobilized nuclease $P_1$ on RNA as a substrate were 0.92% and 1.48%, respectively. Finally, continuous production of 5'-nucleotides by enzymatic hydrolysis of RNA was tried using packed-bed reactor and/or continuous-flow stirred-tank reactor.
탄닌 흡착 크로마토그래피에 의한 Penicillium citrinum Nuclease P1의 부분정제
서원철,임번삼,전문진,엠 써네쓰 ( W . C . Suh,B . S . Lim,M . Chun M . Sernetz ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.1
As a new approach for protein purification, affinity characteristics of tannin for enzyme protein and its applicability to adsorption chromatography were investigated. Crude nuclease P₁ was first purified by fractionation of ammonium sulfate followed by tannin adsorption chromatography. Result showed that adsorption capacity of nuclease P₁ onto one gram of immobilized tannin was 40 ㎎ and recovery yield of the enzyme was 90%. Specific activity of the purified nuclease P₁ increased to 15.6 fold higher than of crude extract, recovering 55.396 of enzyme yield.
Penicillium citrinum 의 Nuclease P1 고정화와 생체 반응기에 의한 누클레오티드의 생산
서원철,임번삼,전문진,엠 써네쓰 ( W . C . Suh,B . S . Lim,M . Chun M . Sernetz ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.1
Nuclease P₁ from Penicillium citrinum was immobilized on cellulose by covalent binding method. Their general properties and applicational possibilities were investigated. Optimum reaction temperature of immobilized nuclease P₁ was 70℃ with broader activity range than that of native enzyme, while optimum pH was shifted to pH 5.0 from pH 5.5 for the native enzyme. Km values of native and immobilized nuclease P₁ on RNA as a substrate were 0.92% and 1.48%, respectively. Finally, continuous production of 5`-nucleotides by enzymatic hydrolysis of RNA was tried using packed-bed reactor and/or continuous-flow stirred-tank reactor.