Literature DB >> 14256

The Bohr effect on the reaction of carbon monoxide with fully oxygenated haemoglobin.

J A Sirs.   

Abstract

1. The rate at which CO displaces O2 from its combination with haemoglobin in solution, has been measured spectrophotometrically, using a rapid-mixing stopped-flow technique. 2. In the presence of CO2, the reaction proceeds by a unimolecular dissociation, with a rate constant r. 3. The relationship of the reciprocal of r to the ratio PO2/PCO is nonlinear, and a different curve is obtained at each CO concentration. 4. Measurements were made of the rate of the reaction when the pH was varied, with constant or varying PCO2. In both situations the value of r was found to have a miximum, for a given PO2/PCO ratio and CO cencentration, at pH 7.2. 5. An analysis of these results suggest that the Bohr effect, of pH and PCO2, is a dynamic equilibrium between four stable tertiary states of each of the alpha and beta chains. Each intermediatory complex has different rate constants for CO and O2.

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Year:  1976        PMID: 14256      PMCID: PMC1307713          DOI: 10.1113/jphysiol.1976.sp011641

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  16 in total

1.  Stopped-flow measurements of CO and O2 uptake by hemoglobin in sheep erythrocytes.

Authors:  J A SIRS; F J ROUGHTON
Journal:  J Appl Physiol       Date:  1963-01       Impact factor: 3.531

2.  Partition of carbon monoxide and oxygen between air and whole blood of rats, dogs and men as affected by plasma pH.

Authors:  T A ALLEN; W S ROOT
Journal:  J Appl Physiol       Date:  1957-03       Impact factor: 3.531

3.  The kinetics of dissociation of the first ligand molecule from fully saturated carboxyhaemoglobin and nitric oxide haemoglobin in sheep blood solutions.

Authors:  Q H GIBSON; F J ROUGHTON
Journal:  Proc R Soc Lond B Biol Sci       Date:  1957-08-24

4.  The carbon monoxide dissociation curve of human blood.

Authors:  N JOELS; L G PUGH
Journal:  J Physiol       Date:  1958-06-18       Impact factor: 5.182

5.  The determination of the individual equilibrium constants of the four intermediate reactions between oxygen and sheep haemoglobin.

Authors:  F J ROUGHTON; A B OTIS; R L LYSTER
Journal:  Proc R Soc Lond B Biol Sci       Date:  1955-08-16

6.  The equilibrium between carbon monoxide and sheep haemoglobin at very high percentage saturations.

Authors:  F J ROUGHTON
Journal:  J Physiol       Date:  1954-11-29       Impact factor: 5.182

7.  Characterization of intermediate states in the ligation of hemoglobin.

Authors:  W H Huestis; M A Raftery
Journal:  Biochemistry       Date:  1973-06-19       Impact factor: 3.162

8.  Stereochemistry of cooperative effects in haemoglobin.

Authors:  M F Perutz
Journal:  Nature       Date:  1970-11-21       Impact factor: 49.962

9.  The effect of temperature on the reaction of carbon monoxide with oxygenated haemoglobin.

Authors:  J A Sirs
Journal:  J Physiol       Date:  1976-08       Impact factor: 5.182

10.  Thermal studies of the rates of the reactions of carbon dioxide in concentrated haemoglobin solutions and in red blood cells. A. The reactions catalysed by carbonic anhydrase. B. The carbamino reactions of oxygenated and deoxygenated haemoglobin.

Authors:  J C Kernohan; F J Roughton
Journal:  J Physiol       Date:  1968-07       Impact factor: 5.182

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