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The Binding of Carbon Monoxide to α and β Chains in Tetrameric Mammalian Hemoglobin

Open AccessPublished:August 25, 1971DOI:https://doi.org/10.1016/S0021-9258(18)61982-9
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      Hemoglobins stripped of organic phosphate by gel filtration and dissolved in 2,2-bis(hydroxymethyl)-2,2',2''-nitrilotriethanol (bis-tris) buffers at pH 7, or in borate buffers at pH 9, show sharp isosbestic points when their reaction with carbon monoxide is examined by the stopped flow method. The time course of the reaction is independent of the wave length of the observing light. In phosphate buffers at pH 7, or on the addition of 2,3-diphosphoglycerate or of inositol hexaphosphate to bis-tris buffers, isosbestic points are no longer found and the time course of the reaction varies with the wave length of the observing light. This result is attributed to differences between the α and β chains. Sheep hemoglobin is exceptional among the mammalian hemoglobins examined because it shows sharp isosbestic points under all conditions tested.

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