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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1997-8-12
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pubmed:abstractText |
Rat erythrocytes subjected to hypotonic-isotonic dialysis, or crosslinking with bifunctional reagents (glutaraldehyde and dimethyl suberimidate hydrochloride) show a high percentage of methemoglobin and decreased oxyhemoglobin content which implies a low oxygen carrying capacity. Such modified cells maintain reversible oxygen binding properties although, they present a high hemoglobin oxygen affinity (low P50) and a diminished cooperativity in binding oxygen to hemoglobin (low n). These results suggest a reduced capacity of liberating oxygen to tissues under low PO2. Changes produced in erythrocytes can not be restored even in the presence of energy (ATP), reduced glutathione and 2,3-bisphosphoglyceric acid during the dialysis process or after crosslinking/permeabilizing treatment.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,3-Diphosphoglycerate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Dimethyl Suberimidate,
http://linkedlifedata.com/resource/pubmed/chemical/Diphosphoglyceric Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaral,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobin H,
http://linkedlifedata.com/resource/pubmed/chemical/Hypotonic Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/Methemoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Oxyhemoglobins
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pubmed:status |
MEDLINE
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pubmed:issn |
0024-3205
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
445-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9244371-2,3-Diphosphoglycerate,
pubmed-meshheading:9244371-Adenosine Triphosphate,
pubmed-meshheading:9244371-Animals,
pubmed-meshheading:9244371-Cross-Linking Reagents,
pubmed-meshheading:9244371-Dialysis,
pubmed-meshheading:9244371-Dimethyl Suberimidate,
pubmed-meshheading:9244371-Diphosphoglyceric Acids,
pubmed-meshheading:9244371-Erythrocytes,
pubmed-meshheading:9244371-Glutaral,
pubmed-meshheading:9244371-Glutathione,
pubmed-meshheading:9244371-Hemoglobin H,
pubmed-meshheading:9244371-Hypotonic Solutions,
pubmed-meshheading:9244371-Male,
pubmed-meshheading:9244371-Methemoglobin,
pubmed-meshheading:9244371-Osmotic Fragility,
pubmed-meshheading:9244371-Oxygen,
pubmed-meshheading:9244371-Oxyhemoglobins,
pubmed-meshheading:9244371-Rats,
pubmed-meshheading:9244371-Rats, Wistar
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pubmed:year |
1997
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pubmed:articleTitle |
Oxygenation capacity of hypotonized and crosslinked rat erythrocytes.
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pubmed:affiliation |
Departamento de Bioquímica y Biología Molecular. Universidad de Alcalá. Campus Universitario, Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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