Interspecies hybrid HbS: complete neutralization of val6(β)-dependent polymerization of human β-chain by pig α-chains

Interspecies hybrid HbS (α2Pβ2S), has been assembled in vitro from pig α-globin and human βS-chain. The α2Pβ2S retains normal tetrameric structure (α2β2) of human Hb and an O2 affinity comparable to that of HbS in 50 mM Hepes buffer; but, its O2 affinity is slightly higher than that of HbS in the pr...

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Veröffentlicht in:	Journal of molecular biology 2000-07, Vol.300 (5), p.1389-1406
Hauptverfasser:	Rao, M.Janardhan, Malavalli, Ashok, Manjula, Belur N, Kumar, Ramesh, Prabhakaran, Muthuchidambaran, Sun, D.Philip, Ho, Nancy T, Ho, Chien, Nagel, Ronald L, Acharya, A.Seetharama
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation - genetics Amino Acid Sequence Amino Acid Substitution - genetics Anemia, Sickle Cell - therapy Animals antisickling globins Binding Sites Dimerization gene therapy Genetic Therapy Globins - chemistry Globins - genetics Globins - metabolism Heme - chemistry Heme - metabolism Hemoglobin, Sickle - chemistry Hemoglobin, Sickle - genetics Hemoglobin, Sickle - metabolism Humans hybrid Hb Hydrogen-Ion Concentration Kinetics Magnetic Resonance Spectroscopy Models, Molecular molecular modeling Oxygen - metabolism Protein Engineering Protein Structure, Quaternary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism semisynthetic chimeric α-chains Static Electricity Swine Valine - genetics Valine - metabolism
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