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Article

Two mutations in recombinant Hb beta F41(C7)Y, K82 (EF6)D show additive effects in decreasing oxygen affinity.

Protein science : a publication of the Protein Society - 1 Jan 1996

Dumoulin A, Kiger L, Griffon N, Vasseur C, Kister I, Génin P, Marden M C, Pagnier J, Poyart C

Abstract excerpt

Based on the properties of two low oxygen affinity mutated hemoglobins (Hb), we have engineered a double mutant Hb (rHb beta YD) in which the beta F41Y substitution is associated with K82D. Functional studies have shown that the Hb alpha 2 beta 2(C7)F41Y exhibits a decreased oxygen affinity relative to Hb A, without a significantly increased autooxidation rate. The oxygen affinity of the natural mutant beta K82D...

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Identifiers

PMID: 8771203
DOI: 10.1002/pro.5560050114
PMCID: PMC2143233

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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