Sigmoid shape of the oxygen equilibrium curve and the P50 of human hemoglobin |
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| Authors: | M. Kobayashi G. Satoh K. Ishigaki |
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| Affiliation: | (1) Department of Biology, Faculty of Science, Niigata University, 950-21 Niigata, (Japan);(2) Information Processing Center, Niigata University, 950-21 Niigata, (Japan) |
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| 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-forth 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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| Keywords: | Hemoglobin cooperativity P50 oxygen affinity Hill coefficient oxygen equilibrium curve |
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