Fixation of various aldehydic dextrans onto human hemoglobin: study of conjugate stability.
Formation and stability of different aldehydic dextran-hemoglobin conjugates were studied. Two types of polymers were used: sulfated or unsulfated oxidized dextrans and 4-carboxamidobenzaldehyde dextran. Periodate-oxidized dextran forms imine and ketoamine linkages by reaction with hemoglobin and the obtained conjugates are not completely stable, as their molecular size increases with time or decreases after incubation with lysine. The sulfated conjugates are more sensitive to lysine action than the unsulfated ones, which is consistent with the decreased possibilities of Amadori rearrangement. Therefore, this proves the importance of ketoamines for ensuring the cohesion of oxidized dextran-based conjugates. Carboxamidobenzaldehyde dextran forms only imine linkages with hemoglobin and the corresponding conjugates possess a marked instability in the absence of reductive treatment. The different types of conjugates could be stabilized by a sodium borohydride treatment in a satisfying manner.
Bonneaux
F
F
Laboratorie de Chimie Physique Macromoléculaire, URA CNRS 494, ENSIC, Nancy, France.
Dellacherie
E
E
D001547:Benzaldehydes / Q000737:chemistry; D003911:Dextrans / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D010084:Oxidation-Reduction
D001547:Benzaldehydes; D003911:Dextrans; D006454:Hemoglobins