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- W2009172803 abstract "Abstract The hybridization behavior of the two electrophoretically variant sheep hemoglobins was studied. Sedimentation-velocity experiments showed that at pH 4.7, and at and above pH 10.0, both variant typs have sedimentation coefficients which are significantly lower than those at pH 7.0, indicating dissociation of the molecules into subunits. Type B dissociates more readily than type A at both acid and alkaline pH. In experiments employing hemoglobins labeled either with [14C]valine or by oxidation to methemoglobin, subunit exchange between variant types was demonstrated, but exchange to the extent predicted on theoretical grounds was not obtained. Experimental evidence indicates that this incomplete hybridization is probably not due to procedural effects. Inadequate dissociation into asymmetric half-molecules or incompatibility between asymmetric half-molecules derived from different variant types seems the most probable explanation. Most or all of the charge different between the two types, approximately four more positive charges per molecule on type B than type A at acid pH, resides in only one of the two kinds of polypeptide chains making up the molecule." @default.
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- W2009172803 date "1962-11-01" @default.
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- W2009172803 title "Molecular hybridization between sheep-hemoglobin variants" @default.
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- W2009172803 doi "https://doi.org/10.1016/0006-3002(62)90153-1" @default.
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