Author： Ookawara Tomomi Eguchi Hironobu Kizaki Takako Nakao Chitose Sato Yuzo Imazeki Nobuo Matsubara Osamu Ohno Hideki Suzuki Keiichiro
Publisher： Informa Healthcare
ISSN： 1071-5762
Source： Free Radical Research, Vol.37, Iss.8, 2003-01, pp. : 823-827
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Abstract
Human extracellular superoxide dismutase (EC-SOD) was purified to homogeneity from lung tissue and the nature of the binding of heparin to EC-SOD was investigated. The enzyme was purified using three column chromatographic steps, and 127 μg of purified EC-SOD was obtained. A specific anti-human EC-SOD antibody was obtained by immunization with the purified enzyme. Western blot analysis of the heparin affinity chromatography product indicated that the presence of the inter-subunit disulfide bond affects the affinity of EC-SOD for heparin. The affinity of EC-SOD for heparin is a very important feature of the enzyme because it controls the distribution of the enzyme in tissues. The present study suggests that, not only the processing of the C-terminal region but inter-subunit disulfide bonds also play a role in determining the tissue distribution of EC-SOD. Moreover, the results obtained here also suggest that the redox state of the tissues might regulate the function of the EC-SOD.
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