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Mécanisme d’action de l’oxyde de carbone sur l’affinité de I’hémoglobine pour l’oxygène

 

作者: D. Vanuxem,   P.J. Weiller,   C. Guillot,   Ch. Grimaud,  

 

期刊: Respiration  (Karger Available online 1982)
卷期: Volume 43, issue 1  

页码: 45-50

 

ISSN:0025-7931

 

年代: 1982

 

DOI:10.1159/000194462

 

出版商: S. Karger AG

 

关键词: 3-Diphosphoglycerate;P50;Stripped hemoglobin;Carboxyhemoglobin;2

 

数据来源: Karger

 

摘要:

The authors have studied the action of carbon monoxide on the affinity of hemoglobin for oxygen by measuring P50 in whole blood and in stripped hemoglobin before and after exposition of blood samples from heavy smokers and polycythemic patients with high levels of HbCO (7.92 ± 0.7%) to hyperbaric oxygen (2.2 ata). The concentration of 2,3-diphosphoglycerate was normal although P50 was significantly lowered, not only in whole blood but also in stripped hemoglobin (2 p < 0.001). Hyperbaric oxygen normalized P50 by removing CO radicals from stripped hemoglobin. This may indicate that CO radicals exert a direct action on the hemoglobin molecule, at least at the HbCO levels studied in this work

 

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