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A Hypothesis for the Increased Oxygen Affinity in Haemoglobin Malmö
Author(s) -
Zak Solomon J.,
Geller Gary R.,
Rrivit William,
Tukey David,
Brimhall Bernadine,
Jones Richard T.,
Bunn H. Franklin,
McCormack Michael
Publication year - 1976
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1976.tb00975.x
Subject(s) - oxygen , chemistry , organic chemistry
S ummary . Haemoglobin Malmöβ 97HisGln , 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 β 93 cysteine and the amide of oxygen of the substituted β 97 glutamine as an explanation for the high oxygen affinity of haemoglobin Malmö.