Some properties of erythrocuprein treated by organic solvents.
The effect of various types of organic solvents on the properties of bovine erythrocuprein was studied. Three organic solvents were found in which the protein is soluble, these were: dimethyl sulfoxide, formamide and N-methylformamide. It was shown that in formamide and dimethyl sulfoxide media the protein possees superoxide dismutase activity, but in N-methylformamide the protein has negligible activity. In organic solvents the substrate (superoxide radical) and solvated electron result in reduction of the protein copper. At high concentrations of superoxide radical or solvated electrons an inactivation of protein and stabilization of superoxide radicals was noted. The stabilization is most pronounced in N-methylformamide. The protein that is reduced by the radical or the solvated electron may be reoxidized by molecular oxygen, the latter being reduced to the superoxide radical.
D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification / Q000378:metabolism; D002417:Cattle; D003300:Copper; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D008667:Metalloproteins / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D012997:Solvents; D013053:Spectrophotometry; D013482:Superoxide Dismutase / Q000097:blood
D001798:Blood Proteins; D008667:Metalloproteins; D012997:Solvents; D003300:Copper; D013482:Superoxide Dismutase