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[Current conception of the Bohr effect].
Poumon Coeur. 1975; 31(4):173-7.PC

Abstract

The molecular mechanism of the Bohr effect is explained according to the molecular model proposed by Perutz et al. The Bohr effect is due to changes in the pK of specific carboxyl and amino groups of the four globin chains following the transition between the deoxy and oxy conformations of the molecule. Carbon dioxide binds to the N terminal valine of the 4 monomers to form carbamino compounds. This carbaminoformation depends upon pH, PCO2 and predominates on deoxygenated haemoglobin. It is lowered when O2 binds to the heme groups (O2 linked carbamino compounds). Through the carbamino compounds Carbon dioxide lowers both the affinity of haemoglobin for O2 and the Bohr effect. Diphosphoglycerate also binds to the haemoglogin molecule. This organophosphate lowers the affinity for O2 but increases the Bohr effect. In whole blood, the Bohr effect is therefore dependent upon pH, O2 saturation, PCO2 and DPG concentration into the red blood cells.

Authors

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Pub Type(s)

English Abstract
Journal Article

Language

fre

PubMed ID

1718

Citation

Poyart, C F., and E Bursaux. "[Current Conception of the Bohr Effect]." Le Poumon Et Le Coeur, vol. 31, no. 4, 1975, pp. 173-7.
Poyart CF, Bursaux E. [Current conception of the Bohr effect]. Poumon Coeur. 1975;31(4):173-7.
Poyart, C. F., & Bursaux, E. (1975). [Current conception of the Bohr effect]. Le Poumon Et Le Coeur, 31(4), 173-7.
Poyart CF, Bursaux E. [Current Conception of the Bohr Effect]. Poumon Coeur. 1975;31(4):173-7. PubMed PMID: 1718.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Current conception of the Bohr effect]. AU - Poyart,C F, AU - Bursaux,E, PY - 1975/1/1/pubmed PY - 1975/1/1/medline PY - 1975/1/1/entrez SP - 173 EP - 7 JF - Le Poumon et le coeur JO - Poumon Coeur VL - 31 IS - 4 N2 - The molecular mechanism of the Bohr effect is explained according to the molecular model proposed by Perutz et al. The Bohr effect is due to changes in the pK of specific carboxyl and amino groups of the four globin chains following the transition between the deoxy and oxy conformations of the molecule. Carbon dioxide binds to the N terminal valine of the 4 monomers to form carbamino compounds. This carbaminoformation depends upon pH, PCO2 and predominates on deoxygenated haemoglobin. It is lowered when O2 binds to the heme groups (O2 linked carbamino compounds). Through the carbamino compounds Carbon dioxide lowers both the affinity of haemoglobin for O2 and the Bohr effect. Diphosphoglycerate also binds to the haemoglogin molecule. This organophosphate lowers the affinity for O2 but increases the Bohr effect. In whole blood, the Bohr effect is therefore dependent upon pH, O2 saturation, PCO2 and DPG concentration into the red blood cells. SN - 0032-5821 UR - https://www.unboundmedicine.com/medline/citation/1718/[Current_conception_of_the_Bohr_effect]_ DB - PRIME DP - Unbound Medicine ER -