Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0409974 (lupus)
 22,386 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The oxygen binding properties of hemoglobin and some hematological parameters in Eskimo dogs (belonging to Canis lupus familiaris) in Ilulissat/Jacobshavn, Greenland were analysed. The average [2,3-DPG] and [Hb] (n = 16) were 3.14 +/- 0.34 mmol l-1 blood and 9.53 +/- 0.65 g dl-1 (1.49 mmol l-1), respectively, giving a stoichiometric ratio of 2.11 mol 2,3-DPG/mol Hb. Oxygen binding analysis carried out on hemolysate in HEPES buffer at 20 and 37 degrees C revealed a high oxygen affinity (1.2 mmHg at pH 7.4, 20 degrees C) in the desalted condition, which decreased markedly in the presence of chloride and 2,3-DPG. A low apparent equilibrium constant for the binding of 2,3-DPG (1.0 x 10(-5) mol l-1) was found at pH 7.2 and 20 degrees C in the absence of chloride. Moreover, we show that chloride ions have an additive effect on oxygen affinity in the concentration range 10-300 mmol l-1 in the presence of 3 mmol l-1 2,3-DPG at low pH and temperature (pH < 7.4 and 20 degrees C). This feature may be of physiological importance to oxygen unloading under acidotic conditions when tissue temperature is low. Thermodynamic analysis reveal that in the presence of 3 mmol l-1 2,3-DPG and 100 mmol l-1 chloride, the Eskimo dog hemoglobin exhibits a low heat of oxygenation, which places this animal close to arctic ruminants with respect to the influence of temperature on oxygen binding in vivo.
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PMID:Functional characterisation of Eskimo dog hemoglobin: I. Interaction of Cl- and 2,3-DPG and its importance to oxygen unloading at low temperature. 917 89

Hemoglobin (Hb) from the Eskimo dog (belonging to Canis lupus familiaris) showed similar Bohr effect (delta log P50/delta pH) to human HbA in the presence of 100 mmol l-1 NaCl at 20 degrees C. The presence of 7% carbon dioxide in the desalted condition caused a positive (reversed) Bohr effect in the pH range 7.1-7.5 on Eskimo dog Hb, whereas in human HbA there was no Bohr effect within this pH range. A positive Bohr effect on Eskimo dog Hb in this condition was also observed at 37 degrees C. This could indicate differences in the pK values of the amino terminal residues of the two hemoglobins, with possible pH-dependent binding of both bicarbonate (HCO(3)-) and carbamate. Analysis of the effect of CO2 on oxygen affinity of Eskimo dog Hb in the pH range 6.7-7.6 in the presence of chloride and/or 2,3-diphosphoglycerate (2,3-DPG) support this theory. Our results indicate a competition between HCO(3)- and Cl- in affecting oxygen binding. Thermodynamic analysis reveals that bicarbonate binding lowers the apparent heat of oxygenation in Eskimo dog Hb nearly as much as chloride does in the presence of 2,3-DPG at physiological pH. This safeguards an effective oxygen unloading at lowered red blood cell concentrations of chloride. Moreover, we show that the oxygen affinity at high O2 saturation is less dependent on temperature in the presence than in the absence of CO2-.
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PMID:Functional characterisation of Eskimo dog hemoglobin: II. The interplay of HCO(3)- and Cl-. 917 90