Complex application of the disc-electrophoresis and gel-filtrations methods for the analysis of carbon oxide influence on the structure of human oxyhemoglobin molecules

Abstract

Chromatographic and electrophoretic properties of samples of human oxy- and
carboxyhemoglobin and their mixes in the ratio 9:1, 5:5 and 1:9 accordingly has been investigated. Joint
application of methods of PAAG disc-electrophoresis and gel-filtration on sephadex has allowed to
establish, that carbon oxide presence promotes turning apoprotein component of hemoglobin molecules.
Replacement О2 on CO results in decrease of heterogeneity of protein structure: at the
electrophoregrammes of HbCO one fraction is found out only, HbO2 has been represented by four
fractions. In preparations of main fraction of HbO2 and HbCO mixes dimeres peculiar to
carboxyhemoglobin was not revealed, in them prevailed tetramerous and monomerous forms similar like
at HbO2. Thus, the effects caused by presence of HbO2, despite of ninefold prevalence hemoglobin
carboxyform in a mixture of hemoproteins were shown