Optical Marking of Alcohol Induced Hemoglobin Modification

TL;DR

This study demonstrates optical methods to detect hemoglobin modifications caused by alcohol consumption, revealing structural changes and their potential biochemical mechanisms in blood proteins.

Contribution

It introduces optical spectroscopy techniques to visualize and analyze alcohol-induced hemoglobin modifications and their biochemical implications.

Findings

Ethanol alters hemoglobin oxygenation kinetics.

Blood from alcoholized rats shows higher dye affinity.

Long-term alcohol intake affects hemoglobin derivative levels.

Abstract

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.