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 language | English |
|---|---|
| Pages (from-to) | 5413-5418 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 250 |
| Issue number | 14 |
| Publication status | Published - 1975 |
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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 journal › Article
}
TY - JOUR
T1 - The binding of CO2 to human hemoglobin
AU - Perrella, M.
AU - Bresciani, D.
AU - Rossi Bernardi, L.
PY - 1975
Y1 - 1975
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0016590903&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0016590903&partnerID=8YFLogxK
M3 - Article
VL - 250
SP - 5413
EP - 5418
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 14
ER -