Three superoxide dismutases have been purified from muscle tissue of the shrimp Macro brachium npponensis. The purification was achieved by thennal treatment, ammonium sulfate fractionation, column chromatogs on DEAE-cellulose 32. The purified enzymes were achieved electrophoresis purification. Their partial characterization has been determined. The first enzyme was CuZnSOD, composed of one subunit of about 66.2kDa, as judged by SDS-polyacrylamide-gel electrophoresis. The absorbance peak of the purified enzyme in ultraviolet region was at 269nm. This enzyme remained stable at 25-45 and pH5-9. The second enzyme was MnSOD (MnSOD-J), composed of one subunit of about 20.2kDa, as judged by SDS-polyacrylamide-gel electrophoresis. The absorbance peak of the purified enzyme in ultraviolet region was at 278nm. This enzyme remained stable at 25-45...
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