Dl. Currell et al., THE FUNCTIONAL-PROPERTIES OF HEMOGLOBIN MODIFIED WITH MELLITIC DIANHYDRIDE - POSSIBLE APPLICATIONS AS A BLOOD SUBSTITUTE, Biomaterials, artificial cells, and immobilization biotechnology, 21(2), 1993, pp. 153-162
Human oxyhemoglobin reacts with mellitic dianhydride to produce a modi
fied protein which shows a reduced oxygen affinity over a wide pH rang
e, a reduced but significant cooperativity, a reduced Bohr effect and
no response to the allosteric effectors: chloride, clofibric acid or i
nositol hexaphosphate. The amount of crosslinking in the modified hemo
globin is approximately 22% suggesting promise as a blood substitute.
Reaction of deoxyhemoglobin with mellitic dianhydride produces a modif
ied protein with reduced response to clofibric acid and a decrease in
oxygen affinity in the presence of inositol hexaphosphate.