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임용표,김병동,Lim, Yong-Pyo,Kim, Byung-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
한 독특한 DNA-수정 효소가 진주조(Pennisetum typhoides) 미토콘드리아에서 분리되었다. 이 효소는 negatively supercoiled pBR322 DNA를 이완시켜 open circular DNA를 주산물로, 또한 linear DNA와 고분자량 multimer complex를 부산물로 만든다. 이 효소는 미토콘드리아의 용성분획에서 DEAE-cellulose 및 Sephacryl S200 SF column chromatography, 그리고 polyacrylamide gel electrophoresis에 의하여 분리되었다. 이 효소는 이가 양이온들 ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$ 및 $Ca^{++}$)을 필요로 하나 ATP는 필요로 하지 않는다. 이 효소는 고농도의 일가 몇 이가 양이온들, EDTA, SDS, 그리고 spermidine에 의해 억제된다. 이 효소의 분자량은 약 70,000으로 추정된다. 이 효소는 박테리아의 topoisomerase I과는 달리 사다리 중간산물을 만들지 않으며, 고분자량 multimer도 생산하므로 topoisomerase와 recombinase의 복합기능 단백질로 추정된다. 이 독특한 효소를 잠정적으로 "신종 토포아이소머레이즈"라 명명한다. A unique DNA-modifying enzyme has been isolated from pearl millet (Pennisetum typhoides) mitochondria. The enzyme relaxes negatively supercoiled pBR322 into an open circular DNA as a major product and also produces a linear DNA and high molecular weight multimer complexes as minor products. The enzyme was isolated from the soluble fraction of mitochondria by DEAE-cellulose and Sephacryl S200 SF column chromatography steps and polyacrylamide gel electrophoresis. The enzyme is dependent on divalent cations ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$, and $Ca^{++}$), and is independent of ATP. The enzyme is inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The molecular weight of this protein is estimated to be about 70,000. The new enzyme, unlike the bacterial topoisomerase I, does not produce ladder intermediate, but also produces high molecular weight multimers. This suggests that the new protein is a mixed functional enzyme of topoisomerase and recombinase. We tentatively call this unique enzyme a novel c1ass of topoisomerase.
진주조 미토콘드리아로 부터 DNA 결합 단백질의 분리와 동정
임용표,김병동 ( Yong Pyo Lim,Byung Dong Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
A DNA-binding protein was isolated from pearl millet (Pennisetum typhoides) mitochondrial DNA. The DNA-binding protein transformed negatively supercoiled pBR322 DNA into an open circle DNA as a major product, and a linear DNA and a high molecular weight multimer as minor products. The reaction was dependent on divalent cations (Mg ^(++), Mn^(++), Zn^(++), and Co^(++), but was independent of ATP. The enzyme reaction was inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The putative multifunctional enzyme is tentatively designated as a new class of topoisomerase, since, unlike the bacterial topoisomerase I, it does not produce the ladder intermediates.
Isolation and Characterization of a DNA-binding Protein from Pearl Millet Mitochondria
임용표,김병동,Lim, Yong-Pyo,Kim, Byung-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
한 DNA-결합 단백질이 진주조 (Pennisetum typhoides)의 미토콘드리아 DNA로부터 분리되었다. 그 DNA결함 단백질은 negatively supercoiled pBR322 DNA를 open circle DNA를 주산물로, linear DNA와 고분자량 multimer를 부산물로 전환시켰다. 반응은 이가 양이온 ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$)을 필요하였으나 ATP를 필요로 하지 않았다. 효소반응은 고농도의 일가 및 이가 양이온, EDTA, SDS, 그리고 spermidine에 의하여 억제되었다. 이 다기능 효소 (topoisomerase, recombinase)는 박테리아 topoisomerase I과는 달리 사다리 중간물질을 만들지 않으므로 잠정적으로 신종의 topoisomerase로 명명한다. A DNA-binding protein was isolated from pearl millet (Pennisetum typhoides) mitochondrial DNA. The DNA-binding protein transformed negatively supercoiled pBR322 DNA into an open circle DNA as a major product, and a linear DNA and a high molecular weight multimer as minor products. The reaction was dependent on divalent cations ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$), but was independent of ATP. The enzyme reaction was inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The putative multifunctional enzyme is tentatively designated as a new class of topoisomerase, since, unlike the bacterial topoisomerase I. it does not produce the ladder intermediates
진주조 미토콘드리아 용성분획의 신종 토포아이소머레이즈 그의 분리와 동정
임용표,김병동 ( Yong Pyo Lim,Byung Dong Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
A unique DNA-modifying enzyme has been isolated from pearl millet (Pennisetum typhoides) mitochondria. The enzyme relaxes negatively supercoiled pBR322 into an open circular DNA as a major product and also produces a linear DNA and high molecular weight multimer complexes as minor products. The enzyme was isolated from the soluble fraction of mitochondria by DEAE-cellulose and Sephacryl S200 SF column chromatography steps and polyacrylamide gel electrophoresis. The enzyme is dependent on divalent cations (Mg^(++), Mn^(++), Zn^(++), Co^(++), and Ca^(++)), and is independent of ATP. The enzyme is inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The molecular weight of this protein is estimated to be about 70,000. The new enzyme, unlike the bacterial topoisomerase I, does not produce ladder intermediate, but also produces high molecular weight multimers. This suggests that the new protein is a mixed functional enzyme of topoisomerase and recombinase. We tentatively call this unique enzyme a novel class of topoisomerase.