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Glutathione S-Transferase ${\rho}$의 정제 및 특성
이재용,한미영,김두식,Lee, Jae-Yong,Han, Mi-Young,Kim, Doo-Sik 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
사람의 적혈구로부터 glutathione S-transferase $\rho$를 순수하게 분리 정제하였다. 황산암모늄 분별 침전에 이어 세단계의 크로마토그라피 분리과정을 거쳐 정제한 glutathione S-transferase $\rho$의 비활성도는 20.8 units/mg이었다. 정제된 효소단백질은 Sephadex G-100 gel filtration과 SDS-polyacrylamide gel 전기영동 분석결과에 의하여 subunit 분자량 24,000인 dimer 구조임을 확인하였으며 측정된 isoelectric pH는 4.6 이었다. 1-chloro-2, 4-dinitrobenzene에 대한 $K_m$, $V_{max}$는 각각 1.1 mM, 1.0mmol/l/min 였고 glutathione에 대해서는 0.3 mM과 0.55mmol/l/min로 관찰되었다. 화학변형 실험의 결과로부터 glutathione S-transferase $\rho$의 촉매가능과 관련된 아미노 group의 존재 가능성을 추정하였다. Glutathione S-transferase $\rho$ (EC 2.5.1.18) has been purified to homogeneity from human erythrocytes. A combination of gel filtration, ion exchange and hydroxylapatite chromatographic procedure yields the specific activity of 20.8 units/mg. The purified enzyme gives a single band corresponding to 24,000 M.W. on a sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme molecule is characterized tone an acidic protein (pI 4.6) having a dimeric structure with 48,000 M.W. composed of identical size of polypeptide chains. Apparent $K_m$ and $V_{max}$ were determined to be 1.1 mM and 1.0 mmol/l/min for 1-chloro-2, 4-dinitro benzene respectively while 0.3 mM and 0.55 mmol/l/min for glutathione. Results obtained from chemical modification studies suggest that essential amino group(s) critically connected to the catalytic function of glutathione S-transferase $\rho$.
Glutathione S - transferase ρ의 정제 및 특성
이재용,한미영,김두식 ( Jae Yong Lee,Mi Young Han,Doo Sik Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
Glutathione S-transferase ρ(EC 2.5.1.18) has been purified to homogeneity from human erythrocytes. A combination of gel filtration, ion exchange and hydroxylapatite chromatographic procedure yields the specific activity of 20.8 units/㎎. The purified enzyme gives a single band corresponding to 24,000 M.W. on a sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme molecule is characterized to be an acidic protein (pl 4.6) having a dimeric structure with 48,000 M.W. composed of identical size of polypeptide chains. Apparent K_m, and V_(max) were determined to be 1.1 mM and 1.0 mmol/1/min for 1-chloro-2,4-dinitro benzene respectively while 0.3 mM and 0.55 mmol/l/min for glutathione. Results obtained from chemical modification studies suggest that essential amino group(s) critically connected to the catalytic function of glutathione S-transferase ρ.