The binding of oxygen (O2) to hemoglobin (HbA) decreases the affinity of HbA for protons (H+) bound at histidine residues and carbon dioxide (CO2) bound chemically as a carbamate at the N-terminus of the HbA (Ferguson and Roughton 1934, Kernohan & Roughton 1968, Klocke 1973, Morrow et al. 1973, Morrow et al. 1976, Tazawa et al. 1983, Kraan & Rispens 1985, Doyle et al. 1987, Mertzlufft & Brandt 1989, Kalhoff et al.1994, Dash & Bassingthwaighte 2010, reviewed in Jensen 2004). This property of HbA is known as the Haldane Effect and facilitates the exchange of CO2 for O2 in the lungs.
Kalhoff, H, Kiwull-Schöne, H, Werkmeister, F, Kiwull, P, Manz, F, Diekmann, L
Visscher, RB, Marshall, RC, Keim, P, Gurd, FR, Morrow, JS
Ferguson, JK, Roughton, FJ
Kernohan, JC, Roughton, FJ
Gill, SJ, Doyle, ML, Di Cera, E, Robert, CH
Dash, RK, Bassingthwaighte, JB
Matthew, JB, Gurd, FR, Morrow, JS, Wittebort, RJ
Kraan, J, Rispens, P
Brandt, L, Mertzlufft, F
Klocke, RA
Tamura, M, Kagawa, T, Mochizuki, M, Tazawa, H
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