The binding of CO2 to human hemoglobin

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

Research output: Contribution to journalArticlepeer-review


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
Issue number14
Publication statusPublished - 1975

ASJC Scopus subject areas

  • Biochemistry


Dive into the research topics of 'The binding of CO2 to human hemoglobin'. Together they form a unique fingerprint.

Cite this