A Hypothesis for the Increased Oxygen Affinity in Haemoglobin Malmö

Solomon J. Zak, Gary R. Geller, William Rrivit, David Tukey, Bernadine Brimhall, Richard T. Jones, H. Franklin Bunn, Michael McCormack

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Haemoglobin Malmöβ97HisGln, a high oxygen affinity haemoglobin which causes secondary erythrocytosis, is transmitted in an autosomal dominant manner. A hypothesis accounting for the high oxygen affinity, hyperbolic oxy‐haemoglobin dissociation curve, and the relatively normal Bohr effect is presented. The purified abnormal haemoglobin from the present family provided biochemical and functional data for this hypothesis based on the allosteric model proposed by Perutz. Experimental results support the formation of a chemical bond between the ‐SH proton of the β93 cysteine and the amide of oxygen of the substituted β97 glutamine as an explanation for the high oxygen affinity of haemoglobin Malmö.

Original languageEnglish (US)
Pages (from-to)101-104
Number of pages4
JournalBritish Journal of Haematology
Volume33
Issue number1
DOIs
StatePublished - May 1976
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Hematology

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