| Abstract: | Spectral characteristics of ferri- and ferroderivatives of myoglobins have been studied in semiwater mammals. Extinction coefficients in the visible range of the spectrum have been determined for different derivatives of the studied heme proteins. It is established that variations in the maxima and minima of different absorption bands are inconsiderable. Close positions of isobestic points have been revealed for a system of oxyglobin and reduced myoglobin obtained from the muscles of the studied animals. Changes in spectral characteristics of methmyoglobins, induced by the effect of different pH, are identical, which evidences for similarity of the surroundings of active site of the studied heme proteins. |
