{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T08:16:35Z","timestamp":1791360995884,"version":"4.3.1"},"reference-count":108,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2004,10,19]],"date-time":"2004-10-19T00:00:00Z","timestamp":1098144000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Acta Physiologica Scandinavica"],"published-print":{"date-parts":[[2004,11]]},"abstract":"<jats:p>\n                    <jats:bold>Abstract<\/jats:bold>\n                    The discovery of the S\u2010shaped O\n                    <jats:sub>2<\/jats:sub>\n                    equilibrium curve and the Bohr effect in 1904 stimulated a fertile and continued research into respiratory functions of blood and allosteric mechanisms in haemoglobin (Hb). The Bohr effect (influence of pH\/CO\n                    <jats:sub>2<\/jats:sub>\n                    on Hb O\n                    <jats:sub>2<\/jats:sub>\n                    affinity) and the reciprocal Haldane effect (influence of HbO\n                    <jats:sub>2<\/jats:sub>\n                    saturation on H\n                    <jats:sup>+<\/jats:sup>\n                    \/CO\n                    <jats:sub>2<\/jats:sub>\n                    binding) originate in the Hb oxy\u2013deoxy conformational change and allosteric interactions between O\n                    <jats:sub>2<\/jats:sub>\n                    and H\n                    <jats:sup>+<\/jats:sup>\n                    \/CO\n                    <jats:sub>2<\/jats:sub>\n                    binding sites. In steady state, H\n                    <jats:sup>+<\/jats:sup>\n                    is passively distributed across the vertebrate red blood cell (RBC) membrane, and intracellular pH (pH\n                    <jats:sub>i<\/jats:sub>\n                    ) changes are related to changes in extracellular pH, Hb\u2010O\n                    <jats:sub>2<\/jats:sub>\n                    saturation and RBC organic phosphate content. As the Hb molecule shifts between the oxy and deoxy conformation in arterial\u2010venous gas transport, it delivers O\n                    <jats:sub>2<\/jats:sub>\n                    and takes up CO\n                    <jats:sub>2<\/jats:sub>\n                    and H\n                    <jats:sup>+<\/jats:sup>\n                    in tissue capillaries (elegantly aided by the Bohr effect). Concomitantly, the RBC may sense local O\n                    <jats:sub>2<\/jats:sub>\n                    demand via the degree of Hb deoxygenation and release vasodilatory agents to match local blood flow with requirements. Three recent hypotheses suggest (1) release of NO from\n                    <jats:italic>S<\/jats:italic>\n                    \u2010nitroso\u2010Hb upon deoxygenation, (2) reduction of nitrite to vasoactive NO by deoxy haems, and (3) release of ATP. Inside RBCs, carbonic anhydrase (CA) provides fast hydration of metabolic CO\n                    <jats:sub>2<\/jats:sub>\n                    and ensures that the Bohr shift occurs during capillary transit. The formed H\n                    <jats:sup>+<\/jats:sup>\n                    is bound to Hb (Haldane effect) while HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    is shifted to plasma via the anion exchanger (AE1). The magnitude of the oxylabile H\n                    <jats:sup>+<\/jats:sup>\n                    binding shows characteristic differences among vertebrates. Alternative strategies for CO\n                    <jats:sub>2<\/jats:sub>\n                    transport include direct HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    binding to deoxyHb in crocodilians, and high intracellular free [HCO\n                    <jats:sub>3<\/jats:sub>\n                    <jats:sup>\u2212<\/jats:sup>\n                    ] (due to high pH\n                    <jats:sub>i<\/jats:sub>\n                    ) in lampreys. At the RBC membrane, CA, AE1 and other proteins may associate into what appears to be an integrated gas exchange metabolon. Oxygenation\u2010linked binding of Hb to the membrane may regulate glycolysis in mammals and perhaps also oxygen\u2010sensitive ion transport involved in RBC volume and pH\n                    <jats:sub>i<\/jats:sub>\n                    regulation. Blood O\n                    <jats:sub>2<\/jats:sub>\n                    transport shows several adaptive changes during exposure to environmental hypoxia. The Bohr effect is involved via the respiratory alkalosis induced by hyperventilation, and also via the pH\n                    <jats:sub>i<\/jats:sub>\n                    change that results from modulation of RBC organic phosphate content. In teleost fish,\n                    <jats:italic>\u03b2<\/jats:italic>\n                    \u2010adrenergic activation of Na\n                    <jats:sup>+<\/jats:sup>\n                    \/H\n                    <jats:sup>+<\/jats:sup>\n                    exchange rapidly elevates pH\n                    <jats:sub>i<\/jats:sub>\n                    and O\n                    <jats:sub>2<\/jats:sub>\n                    affinity, particularly under low O\n                    <jats:sub>2<\/jats:sub>\n                    conditions.\n                  <\/jats:p>","DOI":"10.1111\/j.1365-201x.2004.01361.x","type":"journal-article","created":{"date-parts":[[2004,10,19]],"date-time":"2004-10-19T14:14:58Z","timestamp":1098195298000},"page":"215-227","source":"Crossref","is-referenced-by-count":303,"title":["Red blood cell pH, the Bohr effect, and other oxygenation\u2010linked phenomena in blood O\n                    <sub>2<\/sub>\n                    and CO\n                    <sub>2<\/sub>\n                    transport"],"prefix":"10.1111","volume":"182","author":[{"given":"F. 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