Bovine hemoglobin (Hb) has been proposed as a potential blood substitu
te because of its low intrinsic oxygen affinity in the absence of chlo
ride anions and 2,3-diphosphoglycerate. The use of bovine blood as a s
ource of Hb does not eliminate the risks of viral infections. Biotechn
ology techniques allow to produce modified recombinant Hbs. We have en
gineered human Hb mutants with the aim of mimicking the functional pro
perties of bovine Hb. The argument for this work resides in the crista
llographic studies and in the comparison of human and bovine beta glob
in sequences. The mutant recombinant Hbs exhibit the heterotropic effe
cts of bovine Hb do not exhibit the low intrinsic oxygen affinity of b
ovine Hb.