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Properties of Glutamine Synthetase from Corynebacterium glutamicum
박미선,최순영,김성진,민경희,Park, Mee-Sun,Choi, Soon-Young,Kim, Sung-Jin,Min, Kyung-Hee 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2
Corynebacterium glutamicum의 glutamine synthetase의 성질과 조절을 규명하기 위하여 두 가지의 ion exchange와 gel chromatography를 포함한 6단계를 거쳐 이 효소를 정제하였다. HPLC (TSK-gel)에 의한 이 효소의 분자량은 440,000이었으며, SDS-PAGE에 의하여 측정한 subunit의 분자량이 56,000과 59,000인 두 가지 band를 확인하였으며, 이 중 분자량 59,000의 band는 adenylylated form으로 추정된다. 그러므로 glutamine synthetase는 8개의 subunits으로 구성된 것으로 생각된다. 이 효소 활성의 최적 pH는 8.0이었고, $50^{\circ}C$ 이상의 높은 온도에서는 급격히 효소 활성이 감소하였다. 효소 활성에 $Mn^{2+}$이 필요하며, AMP나 ADP 같은 nuc1eotides가 억제효과를 나타내었다. 이 결과는 이 효소가 energy charge에 의해 조절됨을 알 수 있었다. 또한 L-alanine, ${\beta}-alanine$, glycine, DL-serine, L-histidine의 혼합물은 더욱 효소 활성의 억제 효과를 나타내었다. The glutamine synthetase of Corynebacterium glutamicum was purified using several chromatogrphic procedures involving two ion exchanges and two gel chromatography steps. The molecular weight of the enzyme by HPLC (TSK-gel) was 440,000 daltons. SDS-PAGE revealed that glutamine synthetase consists of polypeptide chains with the identical molecular weight of 56,000. The results of molecular weight suggest that glutamine synthetase is a octamer of subunits with identical molecular weight. The optimal pH of this enzyme was 8.0 and the enzyme activity was rapidly inactivated at the temperature higher than $50^{\circ}C$. $Mn^{2+}$ ion was required for the enzyme activity. Nucleotides such as AMP and ADP were inhibitory, indicating that this enzyme is regulated by energy charge. The data suggest that various mixtures of L-alanine, D-alanine, glycine, DL-serine, and L-histidine was shown along with cumulative inhibition.
Corynebacterium glutamicum 의 glutamate dehydrogenase 의 정제 및 성질
박미선,최순영,김성진,민경희 ( Mee Sun Park,Soon Young Choi,Sung Jin Kim,Kyung Hee Min ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
Glutamate dehydrogenase has been purified from Corynebacterium glutamicum. The purification was carried out by ammonium sulfate fractionation, on DEAE-cellulose, Ultragel ACA-34, DEAE-Sephacel and HPLC (TSK-gel). A molecular weight of 400,000 has been calculated for the enzyme from HPLC gel filtration. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate revealed that glutamate dehydrogenase consists of polypeptide chains with the identical molecular weight of 63,000±5,000. The results of molecular weight determination led us to propose that glutamate dehydrogenase is a hexamer of subunits with identical molecular weight.
Corynebacterium glutamicum 의 glutamine Synthetase 의 정제와 성질
박미선,최순영,김성진,민경희 ( Mee Sun Park,Soon Young Choi,Sung Jin Kim,Kyung Hee Min ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.2
The glutamine synthetase of Corynebacterium glutamicum was purified using several chromatogrphic procedures involving two ion exchanges and two gel chromatography steps. The molecular weight of the enzyme by HPLC (TSK-gel) was 440,000 daltons. SDS-PAGE revealed that glutamine synthetase consists of polypeptide chains with the identical molecular weight of 56,000. The results of molecular weight suggest that glutamine synthetase is a octamer of subunits with identical molecular weight. The optimal pH of this enzyme was 8.0 and the enzyme activity was rapidly inactivated at the temperature higher than 50℃. Mn^(2+) ion was required for the enzyme activity. Nucleotides such as AMP and ADP were inhibitory, indicating that this enzyme is regulated by energy charge. The data suggest that various mixtures of L-alanine, D-alanine, glycine, DL-serine, and L-histidine was shown along with cumulative inhibition.
Purification and Properties of Glutamate Dehydrogenase from Corynebacterium glutamicum
박미선,최순영,김성진,민경희,Park, Mee-Sun,Choi, Soon-Young,Kim, Sung-Jin,Min, Kyung-Hee 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.2
Corynebacterium glutamicum의 glutamate dehydrogenase를 ammonium sulfate 분획, DEAE-cellulose column chromatography, ultragel ACA-34, DEAE-sphacel, HPLC(TSK-gel)를 사용하여 분리 정제하였다. HPLC gel 여과에 의한 이 효소의 분자량은 400,000이었으며, SDS-PAGE에 의한 subunits의 분자량은 $63,000{\pm}5,000$이었다. 분자량 측정의 결과로 glutamate dehydrogenase는 동일한 분자량을 가진 subunits가 6개 있음을 암시하여 주었다. 이 효소의 최적 pH는 8.0이었고, 최적 효소 활성에 대한 ${\alpha}$-ketoglutarate, $NH_4Cl$ 그리고 NADPH의 최적 농도는 각각 20 mM, 100 mM, 0.1 mM 이었다. Glutamate dehydrogenase has been purified from Corynebacterium glutamicum. The purification was carried out by ammonium sulfate fractionation, on DEAE-cellulose, Ultragel ACA-34, DEAE-Sephacel and HPLC (TSK-gel). A molecular weight of 400,000 has been calculated for the enzyme from HPLC gel filtration. Polyacrylamide gel electrophoresis in sodium dodecyl sulfate revealed that glutamate dehydrogenase consists of polypeptide chains with the identical molecular weight of $63,000{\pm}5,000$. The results of molecular weight determination led us to propose that glutamate dehydrogenase is a hexamer of subunits with identical molecular weight.