[Use of phthalocyanine dye in spectroscopic research on the erythrocyte membrane with altered peripheral protein composition].

The absorption spectra of Heliogen Blue (HB) dye were registered on stained ghosts of human red blood cells. The monomer-dimer ratio (M/D) was used as a characteristic of the absorbtion band of HB in the red spectral region. It is determined that incubation of ghosts in the sodium hydrate solution (pH 12) leads to changes in the visible HB spectrum. When the ghosts are stained after NaOH treatment, the M/D value decreases. When stained ghosts are treated with NaOH, the M/D value increases. The decrease in M/D value is due to the increase in HB sorption capacity of the modified membranes; the increase in M/D value is due to the removal of proteins sorbing HB. The appearance of additional sites for HB sorption and the decrease in M/D value in the HB spectrum may be explained by a conformational alteration of the integral proteins or by substitution of some molecules of the peripheral proteins for the HB molecules.