Allosteric properties of haemoglobin beta 41 (C7) Phe-->Tyr: a stable, low-oxygen-affinity variant synthesized in Escherichia coli. |
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| Authors: | V Baudin J Pagnier N Lacaze M T Bihoreau J Kister M Marden L Kiger C Poyart |
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| Affiliation: | Institut National de la Santé et de la Recherche Médicale U299, H?pital de Bicêtre, Le Kremlin-Bicêtre, France. |
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| Abstract: | In human deoxy haemoglobin, the alpha 42(C7)Tyr-residue is hydrogen-bonded to beta 99(G1)Asp which stabilizes the low-oxygen-affinity deoxy conformation. We engineered a haemoglobin with Tyr for Phe at the homologous C7 position in beta-chains. The oxygen affinity of the variant is decreased about two-fold relative to Hb A while keeping similar KR and KT values. This mutant may be a candidate for the development of an artificial oxygen carrier, as it would not require an external effector for significant oxygen unloading in vivo. |
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