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

doi:10.1111/j.1365-2141.1976.tb00975.x

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 journal › Article › peer-review

9 Scopus citations

Abstract

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 β⁹³ cysteine and the amide of oxygen of the substituted β⁹⁷ glutamine as an explanation for the high oxygen affinity of haemoglobin Malmö.

Original language	English (US)
Pages (from-to)	101-104
Number of pages	4
Journal	British Journal of Haematology
Volume	33
Issue number	1
DOIs	https://doi.org/10.1111/j.1365-2141.1976.tb00975.x
State	Published - May 1976
Externally published	Yes

All Science Journal Classification (ASJC) codes

Hematology

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10.1111/j.1365-2141.1976.tb00975.x

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title = "A Hypothesis for the Increased Oxygen Affinity in Haemoglobin Malm{\"o}",

abstract = "Haemoglobin Malm{\"o}β97HisGln, 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 Malm{\"o}.",

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year = "1976",

month = may,

doi = "10.1111/j.1365-2141.1976.tb00975.x",

language = "English (US)",

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T1 - A Hypothesis for the Increased Oxygen Affinity in Haemoglobin Malmö

AU - Zak, Solomon J.

AU - Geller, Gary R.

AU - Rrivit, William

AU - Tukey, David

AU - Brimhall, Bernadine

AU - Jones, Richard T.

AU - Bunn, H. Franklin

AU - McCormack, Michael

PY - 1976/5

Y1 - 1976/5

N2 - 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.

AB - 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.

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A Hypothesis for the Increased Oxygen Affinity in Haemoglobin Malmö

Abstract

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