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- W278458840 abstract "This chapter reviews the biochemical and physiological effects of the incorporation of allosteric effectors of hemoglobin in red blood cells. The amount of O2 that can be released in a particular organ depends on the critical O2 partial pressure characteristic for the organ and on the architecture of the microvasculature. This O2 release capacity is controlled by the microcirculation and molecular parameters of the intracellular Hb. The O2 release capacity can be enhanced by an increase in the co-operability of the Hb molecule; and/or by right shifting of the entire O2-binding curve toward higher O2 partial pressures. An abnormally high affinity of hemoglobin for oxygen shifts the O2-binding curve to the left and the P50 (O2 partial pressure at which 50% saturation of hemoglobin occurs) decreases causing a lower oxygen release to the tissues. In human RBC, the right-shift is controlled by several allosteric mechanisms, such as Bohr effect, 2, 3-bis-phosphoglycerate (DPG), and CO2-binding." @default.
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- W278458840 date "1986-01-01" @default.
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- W278458840 title "Incorporation of Allosteric Effectors of Hemoglobin in Red Blood Cells. Biochemical and Physiological Effects" @default.
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- W278458840 doi "https://doi.org/10.1016/b978-0-08-030800-5.50018-4" @default.
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