SPECIFIC FEATURES OF THE CONDENSATION OF PROTEINS WITH GLUTARIC DIALDEHYDE

The condensation of proteins (hemoglobin or serum albumin) with monome ric glutaric dialdehyde was studied. The absence of stoichiometry in t he consumption of amino groups and aldehyde groups in the reaction mix ture was observed when glutaric dialdehyde was in excess. The decrease in the number of aldehyde groups in solution exceeded the number of m odified amino groups by 6 to 10 times. This may be the result of the f ormation of protein-bound oligomers of glutaric dialdehyde. We suggest that it is the glutaric dialdehyde oligomers linked to different prot ein molecules that form the intermolecular cross-linkages in the prote in conjugates.