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Adaptation of the Oxygen Affinity of Haemoglobin in Acute Hypoxia * , **
Author(s) -
Kleeberg U.R.,
Rühle K.H.,
Schilling M.,
Freitag M.,
Schlehe H.,
Konietzko N.,
Matthys H.
Publication year - 1974
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1974.tb00371.x
Subject(s) - bohr effect , hypoxia (environmental) , oxygen–haemoglobin dissociation curve , chemistry , oxygen , p50 , respiratory system , respiration , hemoglobin , medicine , biophysics , endocrinology , biochemistry , biology , gene , anatomy , organic chemistry , transcription factor
Summary. When the adaptation of the oxygen affinity of haemoglobin (Hb) to acute hypoxia is tested in healthy volunteers with and without Dipyridamole 1 (D), the Bohr‐effect is shown to play the dominant role for the position of the oxygen dissociation curve (ODC). If the Bohr‐effect is eliminated by calculating a pH corrected P 50 , a shift to the right is observed after only 2 hours of continued hypoxia. This decrease of the O 2 ‐affinity of Hb correlates with an increase in red cell 2, 3‐DiphosphogIycerate (DPG). Under D.‐medication the 2, 3‐DPG levels are significantly higher than the controls. The 2% increase of O 2 ‐availability induced by D. however is fully reversed by the Bohr effect. To raise the O 2 supply at the tissue level in acute hypoxia, the human organism prefers an increase in O 2 ‐binding and ‐transport to a decrease in the O 2 ‐affinity of Hb. The continued respiratory alkalosis raises the 2, 3‐DPG level thus gradually compensating for the primary increase in the oxygen affinity of haemoglobin.