사람 융모막 조직에서 Superoxide Dismutase 의 정제 및 성상Purification and Properties of Superoxide Dismutase from Human Chorion
- Authors
- 황윤영; 김홍배; 백광진; 이희성
- Issue Date
- 1991
- Publisher
- 생화학분자생물학회
- Citation
- BMB Reports, v.24, no.4, pp 410 - 417
- Pages
- 8
- Journal Title
- BMB Reports
- Volume
- 24
- Number
- 4
- Start Page
- 410
- End Page
- 417
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66916
- ISSN
- 1976-6696
1976-670X
- Abstract
- 정상 분만한 사람의 융모막 세포질내에 있는 superoxide dismutase(SOD)는 0.8%의 회수율로 332배 정제되었다. Sephadex G-100 gel filtration 및 HPLC에 의한 분자량은 61 kDa이었으며 SDS-PAGE에 의한 subunits의 분자량은 39 kDa, 22 kDa으로써 SOD는 두개의 다른 subunits으로 구성된 dimer 효소였다. 완충액의 pH가 10.0인 경우 효소의 활성이 3.5배 증가했으며, cyanide 농도에 비례해서 효소의 활성이 억제되었으며, azide는 효소 활성에 영향을 주지 못해서 Cu, Zn-SOD의 성상을 나타냈다. 융모막 mitochondria내에 있는 SOD는 0.8%의 회수율로 155배 정제되었다. Sephadex G-100 gel filtration 및 HPLC에 의한 효소의 분자량은 50kDa이었으며, SDS-PAGE에 의한 subunits의 분자량은 25 kDa으로써 두개의 동일한 subunits으로 구성된 dimer 효소였다. 완충액의 pH를 7.8에서 10.0으로 했을 때 효소의 활성이 억제되었으며, azide와 cyanide에 의해서 효소의 활성이 오직 조금만 억제되어 Mn-SOD의 성상을 나타냈다.
The cytosolic superoxide dismutase (SOD) in human chorion, which was obtained on normal delivery, was purified approximately 332-fold with 0.8% recovery. The enzyme was found to be a heterodimer composed of 39 kDa and 22 kDa subunits. The enzyme showed an activation at alkaline pH (10.0) and was inhibited by cyanide but not by azide, which suggests that the cytosolic SOD of human chorion is of a Cu, Zn-SOD type. The mitochondrial SOD of human chorion, which was purified 155-fold with 0.8% recovery, was found to be a homodimer composed of two 25 kDa subunits. In contrast to the cytosolic SOD, the mitochondrial SOD was markedly inhibited by the raise of pH in the reaction mixture from pH 7.8 to pH 10.0, and only slightly inhibited by cyanide and azide. The results suggest that the mitochondrial SOD of human chorion is of a Mn-SOD type as in other tissues.
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