Some recent work on the interactions of oxygen, carbon dioxide and haemoglobin

Roughton, F. J. W.

doi:10.1042/bj1170801b

Cited by 58 publications

(20 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…It should be pointed out in this connexion that the calculation of the bicarbonate concentration in the red cell from rcl-is not affected by the binding of either ion to plasma proteins or haemoglobin as long as it can be assumed that both ions are bound to the same extent. In any event, the binding of bicarbonate ions to haemoglobin appears to be so small (Roughton, 1970;Kilmartin & Rossi-Bernardi, 1971) that it can be ignored for our purposes.…”

Section: Resultsmentioning

confidence: 99%

Carbamino compounds of haemoglobin in human adult and foetal blood

Bauer¹,

Schröder²

1972

The Journal of Physiology

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Carbamino compounds of haemoglobin in human adult and foetal blood

Bauer¹,

Schröder²

1972

The Journal of Physiology

View full text Add to dashboard Cite

“…The classical Bohr effect has been shown to be the result of both H+ binding and CO2 binding as carbamate (Roughton, 1970). Hlastala & Woodson (1975) showed that the contribution of each is critically dependent on the degree of Hb saturation, base excess and 2,3-diphosphoglycerate levels.…”

Section: T H Maren and E R Swenson Discussionmentioning

confidence: 99%

A comparative study of the kinetics of the Bohr effect in vertebrates.

Maren¹,

Swenson²

1980

The Journal of Physiology

View full text Add to dashboard Cite

SUMMARY1. The kinetics of the Bohr effect and the role of carbonic anhydrase were studied in a series of representative vertebrates using a continuous flow rapid reaction apparatus.2. The rates of the Bohr effect in vertebrates are very similar, and differences among classes are manifestations of the ambient temperature.3. Complete carbonic anhydrase inhibition causes a fifteen to fortyfold reduction in the rate of the Bohr effect, sufficient to abolish its occurrence within capillary transit.4. There is a twenty-three-fold (duck) to 360-fold (man) excess of carbonic anhydrase activity in vertebrate red cells for the normal generation of the Bohr effect.5. When carbonic anhydrase is inhibited and CO2 hydration becomes rate limiting, the stoichiometry of the Bohr effect (Alog po2/ApH) is revealed in the ratio of the rates of proton formation in red cells to 02 release from haemoglobin.

show abstract

“…On the other hand, hemoglobin's ability to bind carbon dioxide is a necessary process to allow for removal of carbon dioxide and byproducts from the system. Because carbon dioxide occupies a different binding site on the hemoglobin molecule, this type of ligand binding is allosteric in nature (Christiansen et al, 1914;Roughton, 1970).…”

Section: Reversible Oxygenation Of Hemoglobinmentioning

confidence: 99%

Iron Deficiency Anemia: A Public Health Problem of Global Proportions

Charles¹

2012

Public Health - Methodology, Environmental and Systems Issues

View full text Add to dashboard Cite

Some recent work on the interactions of oxygen, carbon dioxide and haemoglobin

Cited by 58 publications

References 18 publications

Carbamino compounds of haemoglobin in human adult and foetal blood

Carbamino compounds of haemoglobin in human adult and foetal blood

A comparative study of the kinetics of the Bohr effect in vertebrates.

Iron Deficiency Anemia: A Public Health Problem of Global Proportions

Contact Info

Product

Resources

About