FUNCTIONAL-PROPERTIES OF BETA(NA1)VAL-DELETED,(NA2)HIS -] MET HEMOGLOBIN SYNTHESIZED IN ESCHERICHIA-COLI

Authors
BAUDIN V BIHOREAU MT KISTER J MARDEN M PAGNIER J POYART C
Citation
V. Baudin et al., FUNCTIONAL-PROPERTIES OF BETA(NA1)VAL-DELETED,(NA2)HIS -] MET HEMOGLOBIN SYNTHESIZED IN ESCHERICHIA-COLI, Artificial cells, blood substitutes, and immobilization biotechnology, 22(3), 1994, pp. 739-745
Citations number
10
Categorie Soggetti
Engineering, Biomedical","Materials Science, Biomaterials
Journal title
Artificial cells, blood substitutes, and immobilization biotechnology → ACNP
ISSN journal
10731199
Volume
22
Issue
3
Year of publication
1994
Pages
739 - 745
Database
ISI
SICI code
1073-1199(1994)22:3<739:FOB-MH>2.0.ZU;2-E
Abstract
Bovine Hb (hemoglobin) has a low oxygen affinity in the absence of chl oride 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 methionin e for histidine at the beta NA2 position as previously suggested by Pe rutz and Imai in 1980. Our results show that the artificial mutant exh ibits some of the characteristics of bovine Hb but does not show the l ow oxygen affinity which is measured in bovine blood.