  It has been shown that conformational modifications of Hb induced by ethanol
consumption can be visualized in optical spectra studying oxygenation kinetics
of hemoglobin or mixing hemoglobin with Cibacron blue dye. Better dye affinity
of blood proteins extracted from alcoholised rats with respect to those from
non-alcoholised ones confirms that ethanol and its metabolites induce
structural pathologies in blood protein molecules. The detected changes for the
case of the posterity of intoxicated animals may be explained as a
post-translation modification, as well as a disturbance of the structure and
function of tissue cellular gene mechanism for the blood creation. It is
established that alcohol intake during first four months leads to the decrease
of fractional weight of oxyhemoglobin and to the increase of methemoglobin
amount in blood. Further alcohol consumption is accompanied by recovering of
the normal level of hemoglobin derivatives in blood. Normalization of the
fractional weight of hemoglobin derivatives in blood after durable (longer than
5-6 months) ethanol intoxication is most probably due to the activation of the
enzyme (acetaldehyde dehydrogenase) system, lowering the level of acetaldehydes
in blood.
