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Sigmoid shape of the oxygen equilibrium curve and the P50 of human hemoglobin (1994)

Kobayashi, M. ; Satoh, G. ; Ishigaki, K.

Springer

Cellular and molecular life sciences 50 (1994), S. 705-707

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ISSN: 1420-9071

Keywords: Hemoglobin ; cooperativity ; P50 ; oxygen affinity ; Hill coefficient ; oxygen equilibrium curve

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01919366

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