[Preparation of electrophoretically homogeneous erythrocuprein and its thermodenaturation]

The procedure for isolation of electrophoretically homogeneous preparation of erythrocuprein from 17 1 blood batch was described. The preparation had absorbtion value, A260/A680, of 25-26. The protein completely retains superoxide dismutase activity after treatment 7 min. at 75 degrees C. The heating of protein solution at 100 degrees C bring about autoreduction of protein copper as demonstrated by decreasing optical and EPR-spectral intensities. The reduced protein was oxidized in aerobic condition and oxidized preparation had optical and EPR-spectra differ from those of the native protein the activy being decreased.