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Updated: Aug 2, 2026

A Facile and Efficient Approach for the Production of Reversible Disulfide Cross-linked Micelles
Published on: December 23, 2016
Synthesis, physico-chemical and biological properties of crosslinked modified hemoglobin
N P Kuznetsova1, L R Gudkin, R N Mishaeva
1Institute of Macromolecular Compounds of Russian Academy of Sciences, St. Petersburg, Russia.
Abstract:
Polymer aspects of polycondensation of pyridoxylated hemoglobin with glutaraldehyde have been considered. On the basis of the investigation of reaction kinetics, the mechanism of chemical crosslinking of hemoglobin molecules into oligohemoglobin is proposed. Owing to the statistical character of the reaction, the resulting macromolecules are polydisperse with respect to the degree of modification of hemoglobin amino groups, and size of oligohemoglobin molecules. The formation of hemoglobin oligomers was studied by varying the following reaction conditions: pH, the components ratio, and their concentrations. It is shown that the net electric charge of the oligohemoglobin molecule depends on the terminating agents. However, these agents have no effect on the electrophoretic mobility of erythrocytes in oligohemoglobin solutions. The efficiency of oxygen transport of these solutions is close to that of human blood erythrocytes. Oligohemoglobin circulation in the blood of animals after intravenous infusion leads to rapid removal of low molecular weight fractions from blood and to the accumulation of high molecular weight fractions in plasma. The period of half-release of oligohemoglobin from the organism is 14-16 h.
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