The binding of CO2 to human hemoglobin

M. Perrella, D. Bresciani, L. Rossi Bernardi

Research output: Contribution to journalArticle

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Abstract

CO2 dissociation curves of concentrated human deoxy and carbon monoxyhemoglobin at 37°, pH 7.6 to 7.0, pCO2 = 10 to 160 mm Hg, have been obtained by a rapid mixing and ion exchange technique. The CO2 dissociation curves for deoxyhemoglobin can only be fitted by assuming 2 classes of binding sites for carbon dioxide. The simplest way to account for the experimental data is to assume that the α amino groups of the α and β chains react with carbon dioxide with affinities that differ by at least a factor of 3. No difference in reactivity with CO2 was found among the 4 terminal α amino groups of carbon monoxyhemoglobin.

Original languageEnglish
Pages (from-to)5413-5418
Number of pages6
JournalJournal of Biological Chemistry
Volume250
Issue number14
Publication statusPublished - 1975

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Carbon Dioxide
Hemoglobins
Carbon
Ion Exchange
Ion exchange
Binding Sites
deoxyhemoglobin

ASJC Scopus subject areas

  • Biochemistry

Cite this

The binding of CO2 to human hemoglobin. / Perrella, M.; Bresciani, D.; Rossi Bernardi, L.

In: Journal of Biological Chemistry, Vol. 250, No. 14, 1975, p. 5413-5418.

Research output: Contribution to journalArticle

Perrella, M, Bresciani, D & Rossi Bernardi, L 1975, 'The binding of CO2 to human hemoglobin', Journal of Biological Chemistry, vol. 250, no. 14, pp. 5413-5418.
Perrella, M. ; Bresciani, D. ; Rossi Bernardi, L. / The binding of CO2 to human hemoglobin. In: Journal of Biological Chemistry. 1975 ; Vol. 250, No. 14. pp. 5413-5418.
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