[The species characteristics of the intramolecular structure of hemoglobin in vertebrates].

Using fluorescence spectroscopy species peculiarity of hydrophobic and microviscosity degree in central and peripheral molecular areas of the main electrophoretic haemoglobin fractions in representatives of different vertebrate classes gas been studied. It is established that central areas of haemoglobin molecule are characterised by twice lesser variability of size and hydrophobic degree and 2.4 times greater variability of package strength as compared with peripheral areas of protein globule.