| Literature DB >> 1390926 |
V Baudin1, J Pagnier, N Lacaze, M T Bihoreau, J Kister, M Marden, L Kiger, C Poyart.
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.Entities:
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Year: 1992 PMID： 1390926 DOI： 10.1016/0167-4838(92)90029-d
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002