PHYSICOCHEMICAL PROPERTIES OF HEMOGLOBIN LIGAND FORMS UNDER EXPERIMENTAL STREPTOZOTOCIN-INDUCED DIABETES AND ALCOHOL INTOXICATION
DOI: http://dx.doi.org/10.30970/sbi.1102.527
Abstract
The study of hemoglobin affinity to oxygen, oxygen capacity and the content of ligand forms has been conducted in hemolyzates of rat peripheral blood at chronic alcohol intoxication models and experimental diabetes mellitus. The findings revealed that at alcohol intoxication both hemoglobin affinity to oxygen and hemoglobin oxygen capacity validly decrease, whereas at experimental streptozotocin-induced diabetes hemoglobin the affinity to oxygen increases and oxygen capacity is quite high. The results of study demonstrated that sulf- and methemoglobin levels rise under alcohol intoxication and sulf-, met- and carboxyhemoglobin levels rise under experimental diabetes mellitus. We have also undertaken study of hemoglobin affinity to oxygen, oxygen capacity and the ratio of hemoglobin ligand forms in alcoholics and healthy donors. A valid increase in sulf- and methemoglobin and a decrease in hemoglobin affinity to oxygen in alcoholics (32.50±0.45 versus 28.60±0.54 mm Hg in the control group) with insignificant changes in oxygen capacity were revealed. Since minor ligand forms contribute to the affinity of total hemoglobin to oxygen, their quantitative characteristics are essential. Thus, data on absorption spectra which characterize nitrosyl-hemoglobin ligand form and transition of deoxy- and methemoglobin into nitrosyl-hemoglobin have been collected. A combined absorption spectrum of nitrosyl-hemoglobin has been built based on the statistical data set deoxyhemoglobin and its full transition into nitrosyl-hemoglobin (60 analyses) in the examined wavelength range. The article provides the results of the comparative analysis of electronic absorption spectra characteristic peaks of six hemoglobin ligand forms taken from peripheral blood in healthy donors in 450–750 nm wavelength range. The studies can be a pre-requisite for the development of methods for determining six hemoglobin ligand forms in a single blood sample.
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