Article
Roles of alpha 114 and beta 87 amino acid residues in the polymerization of hemoglobin S: implications for gene therapy.
Journal of molecular biology - 1 Nov 1996
Ho C, Willis B F, Shen T J, Dazhen N T, Sun D P, Tam M F, Suzuka S M, Fabry M E, Nagel R L
Abstract excerpt
Three novel recombinant mutants of sickle hemoglobin (Hb S, beta 6Glu-->Val) have been constructed to assess the role of proline at alpha 114 and threonine at beta 87 in the polymerization of deoxygenated Hb S. Using the hemoglobin expression system (pHE2) designed in our laboratory, four plasmids were expressed separately in Escherichia coli to produce the four recombinant hemoglobins: r Hb S (beta 6Glu-->Val);...
Topics
- Adult
- Anemia, Sickle Cell
- Escherichia coli
- Fetal Hemoglobin
- Genetic Therapy
- Hemoglobin A
- Hemoglobin, Sickle
- Humans
- Magnetic Resonance Spectroscopy
- Mutation
- Oxygen
