Standard and pH-affected hemoglobin-O2 binding curves of Sprague-Dawley rats under normal and shifted P50 conditions |
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Affiliation: | 1. Department of Surgery, University of Adelaide, The Queen Elizabeth Hospital, Woodville, South Australia, Australia;2. Department of Hepatobiliary Surgery, Leicester General Hospital, Leicester, United Kingdom |
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Abstract: | - 1.1. The oxygen saturation (SO2) was determined of Sprague-Dawley rat blood having increased hemoglobin (Hb)-O2 affinity (P50 < 37mmHg) or capacity (Cmax) over a range of pH's.
- 2.2. Rats were untreated (K), or had passed 14 d drinking 0.5% saline (C; ctrl) or NaOCN (N; chronically low P50 high Cmax), 5000m altitude acclimatization (H; high Cmax), or exchange transfusion with OCN−-Hb red cell blood (X; acutely low P50).
- 3.3. The P50 [mmHg], Hill's “n”, and Cmax [ml O2/100 ml], measured after tonometry, were 36.0, 2.60 and 20.6 (K), 32.6, 2.50 and 21.8 (C), 18.3, 2.35 and 23.9 (N), 36.0, 2.60 and 29.4 (H), and 24.9, 2.73 and 22.3 (X).
- 4.4. Oxygen dissociation curves (ODC's), derived from simultaneous SO2 and PO2 measurements during deoxygenation (PO2: 100-0 mmHg) of blood (normal and acidified with CO2 or lactic acid), delivered Bohr coefficients (BCCO2, BCLac) each differing between groups (C vs N) above SO2 50%; within groups BCCO2 vs BCLac differed at SO2 10–90% (P < 0.05).
- 5.5. Group-specific ODC's and pH-shifted curves (± 0.05, ± 0.10 and ±0.15 units from 7.4, relying on BCCO2) are plotted for direct reading of SO2 and, with Cmax, accurate data on blood O2 content are obtained; corrections for lactic acidosis are discussed.
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