Removal of Superoxide Dismutase Activity from Cytochrome C |
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| Authors: | George L. Tritsch |
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| Affiliation: | Department of Surgical Oncology , Roswell Park Memorial Institute New York State Department of Health Buffalo , NY, 14263 |
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| Abstract: | Commercially available cytochrome c contains sufficient superoxide dismutase activity to reduce its sensitivity in superoxide anion detection. A single passage through a column of Sephadex G-50 removes the superoxide dismutase, and appreciably increased the ability of cytochrome c to detect superoxide. |
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| Keywords: | Alkaline protease Bacillus clausii Enzyme purification and characterisation Serine protease |
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