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• W116351894 abstract "Abstract The equilibria and the kinetics of reactions of human with ligands have been studied over a large range of protein concentration in the presence of triethylamine hydrochloride, which favors dissociation of into subunits. The extent of dissociation was determined by ultracentrifuge measurements on the same solutions. The results show that: (a) the oxygen equilibrium of changes only slightly as the triethylamine hydrochloride concentration is increased up to 4 m; specifically, ligand binding is still strongly cooperative even at low protein concentration, at which sedimentation data indicate a large dissociation of the deoxy derivative into dimers and of the oxy one into monomers; (b) the kinetic behavior of in rapid mixing experiments does not change in 2 m triethylamine hydrochloride in respect to normal conditions; (c) the quickly reacting hemoglobin in flash photolysis experiments is not correlated in any simple way with the fraction of dimers nor is it entirely restricted to monomers. The results lead once again to the conclusion that the free αβ dimers show all the characteristic features of ligand binding to and indicate that even in the tetramer they may represent the fundamental unit of function." @default.
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• W116351894 date "1971-03-01" @default.
• W116351894 modified "2023-09-28" @default.
• W116351894 title "Studies on the Relations between Molecular and Functional Properties of Hemoglobin" @default.
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• W116351894 doi "https://doi.org/10.1016/s0021-9258(18)62391-9" @default.
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• W116351894 hasPublicationYear "1971" @default.
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