Thermal stabilities of hemoglobins crosslinked with different length reagents.

Bis(3,5-dibromosalicyl) succinate and glutarate were used to crosslink met-, oxy- and deoxyhemoglobins. The added flexibility of these reagents compared to the fumarate analog resulted in a more heterogeneous product but did not greatly affect the maximum thermal stability of the crosslinked hemoglobins.