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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1990-7-3
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pubmed:abstractText |
1. The oxygen binding properties of hemolyzed bear blood were studied in 0.1 M Tris and 0.1 M Hepes buffer with respect to the possible effects of temperature, pH, pCO2, 2,3-DPG, and chloride ions. 2. There was a significant Bohr shift with a Bohr factor (delta log P50/delta pH) of the magnitude of -0.5. The temperature sensitivity expressed by the apparent heat of oxygenation minus the heat of oxygen in solution was about -8.1 kcal/mol at pH 7.4. 3. Chloride ions decreased the oxygen affinity in the concentration range 50-200 mM, and there was a marked increase in the co-operativity of oxygenation up to a chloride concentration of about 200 mM. 4. There were no effects of pCO2 and 2,3-DPG in the presence of 200 mM Cl-, while in the absence of Cl-, 2,3-DPG had the same effect as 200 mM Cl- at 37 degrees C and pH 7.4. 5. Our results suggests at least two different binding sites for the chloride ion, one high affinity site which may also bind 2,3-DPG in the absence of chloride, and one or more low affinity sites, which only binds chloride. 6. The results further show, that a chloride shift of about 33 mM may account for as much as a 40% increase in O2 unloading, without taking into account the additional effect of the Bohr shift.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,3-Diphosphoglycerate,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorides,
http://linkedlifedata.com/resource/pubmed/chemical/Diphosphoglyceric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen
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pubmed:status |
MEDLINE
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pubmed:issn |
0305-0491
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
95
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
865-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2111752-2,3-Diphosphoglycerate,
pubmed-meshheading:2111752-Animals,
pubmed-meshheading:2111752-Binding Sites,
pubmed-meshheading:2111752-Carbon Dioxide,
pubmed-meshheading:2111752-Carnivora,
pubmed-meshheading:2111752-Chlorides,
pubmed-meshheading:2111752-Diphosphoglyceric Acids,
pubmed-meshheading:2111752-Hemoglobins,
pubmed-meshheading:2111752-Hydrogen-Ion Concentration,
pubmed-meshheading:2111752-Male,
pubmed-meshheading:2111752-Oxygen,
pubmed-meshheading:2111752-Ursidae
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pubmed:year |
1990
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pubmed:articleTitle |
The chloride shift may facilitate oxygen loading and unloading to/from the hemoglobin from the brown bear (Ursus arctos L.).
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pubmed:affiliation |
Zoological Laboratory, University of Bergen, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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