[Transfer of functional properties from bovine hemoglobin to human hemoglobin].

Bovine hemoglobin (Hb) has been proposed as a potential blood substitute because of its low intrinsic oxygen affinity in the absence of chloride anions and 2,3-diphosphoglycerate. The use of bovine blood as a source of Hb does not eliminate the risks of viral infections. Biotechnology techniques allow to produce modified recombinant Hbs. We have engineered human Hb mutants with the aim of mimicking the functional properties of bovine Hb. The argument for this work resides in the crystallographic studies and in the comparison of human and bovine beta globin sequences. The mutant recombinant Hbs exhibit the heterotropic effects of bovine Hb do not exhibit the low intrinsic oxygen affinity of bovine Hb.