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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ho, Nancy T. Tam, Tsuey Chyi S. Ho, Chien Tam, Ming F. Simplaceanu, Virgil Zou, Ming |
| Description | Author Affiliation: Tam MF ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.); Tam TC ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.); Simplaceanu V ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.); Ho NT ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.); Zou M ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.); Ho C ( From the Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213 chienho@andrew.cmu.edu.) |
| Abstract | The unliganded tetrameric Hb S has axial and lateral contacts with neighbors and can polymerize in solution. Novel recombinants of Hb S with single amino acid substitutions at the putative axial (recombinant Hb (rHb) (ßE6V/ H20R) and rHb (ßE6V/ H20Q)) or lateral (rHb (ßE6V/ H50Q)) or double amino acid substitutions at both the putative axial and lateral (rHb (ßE6V/ H20R/ H50Q) and rHb (ßE6V/ H20Q/ H50Q)) contact sites were expressed in Escherichia coli and purified for structural and functional studies. The (1)H NMR spectra of the CO and deoxy forms of these mutants indicate that substitutions at either His-20 or His-50 do not change the subunit interfaces or the heme pockets of the proteins. The double mutants show only slight structural alteration in the ß-heme pockets. All mutants have similar cooperativity (n50), alkaline Bohr effect, and autoxidation rate as Hb S. The oxygen binding affinity (P50) of the single mutants is comparable with that of Hb S. The double mutants bind oxygen with slightly higher affinity than Hb S under the acidic conditions. In high salt, rHb (ßE6V/ H20R) is the only mutant that has a shorter delay time of polymerization and forms polymers more readily than Hb S with a dextran-Csat value of 1.86 ± 0.20 g/dl. Hb S, rHb (ßE6V/ H20Q), rHb (ßE6V/ H50Q), rHb (ßE6V/ H20R/ H50Q), and rHb (ßE6V/ H20Q/ H50Q) have dextran-Csat values of 2.95 ± 0.10, 3.04 ± 0.17, 11.78 ± 0.59, 7.11 ± 0.66, and 10.89 ± 0.83 g/dl, respectively. rHb (ßE6V/ H20Q/ H50Q) is even more stable than Hb S under elevated temperature (60 °C). |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 35 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-08-28 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Hemoglobin, Sickle Genetics Metabolism Mutation Chemistry Histidine Kinetics Oxidation-Reduction Oxygen Polymerization Proton Magnetic Resonance Spectroscopy Recombinant Proteins Solubility Temperature Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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