Functional properties of beta(NA1)Val-deleted,(NA2)His-->Met hemoglobin synthesized in Escherichia coli.
Bovine Hb (hemoglobin) has a low oxygen affinity in the absence of chloride ions and DPG. Because of the increasing interest of this Hb as a potential blood substitute we have engineered a human Hb mutant with the aim of mimicking the functional properties of bovine Hb. This was achieved by deleting residue beta NA1 Val and substituting a methionine for histidine at the beta NA2 position as previously suggested by Perutz and Imai in 1980. Our results show that the artificial mutant exhibits some of the characteristics of bovine Hb but does not show the low oxygen affinity which is measured in bovine blood.
Baudin
V
V
INSERM U299 Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.
Bihoreau
M T
MT
Kister
J
J
Marden
M
M
Pagnier
J
J
Poyart
C
C
D000818:Animals; D001802:Blood Substitutes / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D004926:Escherichia coli / Q000235:genetics; D006454:Hemoglobins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D016297:Mutagenesis, Site-Directed; D010100:Oxygen / Q000378:metabolism; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion
D001802:Blood Substitutes; D006454:Hemoglobins; D011993:Recombinant Fusion Proteins; D010100:Oxygen