title: Possibilities of Using Fetal Hemoglobin as a Platform for Producing Hemoglobin-Based Oxygen Carriers (HBOCs).
abstract: The expression levels of fetal hemoglobin (HbF) in bacterial recombinant systems are higher compared with normal adult hemoglobin (HbA). However, heme disorientation in globins are often observed in recombinant production processes, both for HbA and HbF, although the degree of heme oriental disorder is much lower for HbF. In addition, the heme disorientation can be converted to a normal conformation by an oxidation-reduction process. A chromatographic cleaning process involving a strong anion exchanger can be utilized to remove such unstable and nondesirable forms of Hb.
authors.affiliation: Pure and Applied Biochemistry, Department of Chemistry, Lund University, 221 00, Lund, Sweden.
authors.forename: Khuanpiroon
authors.initials: K
authors.lastname: Ratanasopa
authors.affiliation: Biochemistry and Structural Biology, Department of Chemistry, Lund University, 221 00, Lund, Sweden.
authors.forename: Tommy
authors.initials: T
authors.lastname: Cedervall
authors.affiliation: Pure and Applied Biochemistry, Department of Chemistry, Lund University, 221 00, Lund, Sweden. Leif.Bulow@tbiokem.lth.se.
authors.forename: Leif
authors.initials: L
authors.lastname: Bülow
mesh_terms: D002942:Circular Dichroism; D005319:Fetal Hemoglobin / Q000032:analysis / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D010100:Oxygen / Q000378:metabolism*
chemical_list: D006454:Hemoglobins; D005319:Fetal Hemoglobin; D010100:Oxygen
keywords: Autooxidation; Circular dichroism; E. coli; Heme; Hemoglobin purification