Literature DB >> 8070528

Sigmoid shape of the oxygen equilibrium curve and the P50 of human hemoglobin.

M Kobayashi1, G Satoh, K Ishigaki.   

Abstract

The fractional saturation of hemoglobin with oxygen was plotted against P/P50 and the slope of the abscissa at 1 was calculated for 38 OEC data sets of human Hb A. There was a linear correlation between the slope and the Hill coefficient (nmax), and the slope was about one-fourth that of nmax. This implies that the slope of the abscissa at 1 of Y vs P/P50 plot can provide information about the magnitude of cooperativity in hemoglobin oxygen binding.

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Year:  1994        PMID: 8070528     DOI: 10.1007/bf01919366

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  7 in total

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Authors:  J WYMAN
Journal:  Adv Protein Chem       Date:  1964

2.  Allosteric proteins and cellular control systems.

Authors:  J MONOD; J P CHANGEUX; F JACOB
Journal:  J Mol Biol       Date:  1963-04       Impact factor: 5.469

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Authors:  K Imai; T Yonetani
Journal:  J Biol Chem       Date:  1975-03-25       Impact factor: 5.157

4.  Purification and allosteric properties of yeast pyruvate kinase.

Authors:  R Haeckel; B Hess; W Lauterborn; K H Wüster
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1968-05

5.  Analysis of oxygen equilibrium of hemoglobin and control mechanism of organic phosphates.

Authors:  I Tyuma; K Imai; K Shimizu
Journal:  Biochemistry       Date:  1973-04-10       Impact factor: 3.162

6.  Linkage between carbon dioxide binding and four-step oxygen binding to hemoglobin.

Authors:  K Imaizumi; K Imai; I Tyuma
Journal:  J Mol Biol       Date:  1982-08-25       Impact factor: 5.469

7.  Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus.

Authors:  K Imai
Journal:  Methods Enzymol       Date:  1981       Impact factor: 1.600

  7 in total

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