Surface modification of diaspirin cross-linked hemoglobin (DCLHb) with chondroitin-4-sulfate derivatives. Part 1

Synthetic methodology was developed for the preparation of chondrotin-4-sul fate reagents that could be specifically attached to the surface of diaspir in cross-linked hemoglobin (DCLHb), a chemically stabilized human hemoglobi n. The surface-modified hemoglobin solutions had a significantly higher col loidal osmotic pressures (COP) than DCLHb. The P-50 of the modified DCLHb w as dependent upon the reactive end group of the chondrotin-4-sulfate reagen ts that was used for the protein modification. Modification of DCLHb with t he chondroitin-4-sulfate derivatives containing the maleimide end group 23 provided a hemoglobin with a P50 value of 23 mmHg, while the P-50 of hemogl obins prepared from chondroitin-4-sulfate derivatives containing the aldehy de end group 13 and 18 remained unchanged from that of DCLHb.