Bibliographic Details
| Title: |
Extracellular superoxide dismutase exists as an octamer |
| Authors: |
Due, Anne V.1, Petersen, Steen V.1, Valnickova, Zuzana1, Østergaard, Louise1, Oury, Tim D.2, Crapo, James D.3, Enghild, Jan J.1 jje@mb.au.dk |
| Source: |
FEBS Letters. Feb2006, Vol. 580 Issue 5, p1485-1489. 5p. |
| Subjects: |
Superoxide dismutase, Proteins, Aorta |
| Abstract: |
Abstract: Human extracellular superoxide dismutase (EC-SOD) is involved in the defence against oxidative stress induced by the superoxide radical. The protein is a homotetramer stabilised by hydrophobic interactions within the N-terminal region. During the purification of EC-SOD from human aorta, we noticed that material with high affinity for heparin–Sepharose formed not only a tetramer but also an octamer. Analysis of the thermodynamic stability of the octamer suggested that the C-terminal region is involved in formation of the quaternary structure. In addition, we show that the octamer is composed of both aEC-SOD and iEC-SOD folding variants. The presence of the EC-SOD octamer with high affinity may represent a way to influence the local concentration of EC-SOD to protect tissues specifically sensitive to oxidative damage. [Copyright &y& Elsevier] |
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| Database: |
Engineering Source |
