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• W2028762351 abstract "The theory that the αβ dimer is the functional unit of cooperativity in hemoglobin has been tested by determination of the oxygen equilibrium curve of stable deoxy dimers, obtained by the addition of 0.9 M MgCl 2 to human des-Arg 141α-hemoglobin. Cooperativity was absent in this medium, but was regained on transfer of the hemoglobin to a dilute phosphate buffer, where tetramers reformed. X-ray analysis of crystals of oxy- and deoxy-des-Arg hemoglobins showed that the removal of Arg 141α would leave the structure of αβ dimers unchanged. Nonreactivity of the sulfhydryl groups at 112β proved that the subunits in deoxy dimers form the same contact as in oxy dimers, namely α 1 β 1 , and that no significant dissociation into free subunits occurs in 0.9 M MgCl 2 . The absorption spectrum of the deoxy dimers corresponded to the sum of the spectra of the free deoxy α and β subunits, and was different from that of the deoxy tetramer, showing the constraining salt bridges formed by the C-terminal residues in the tetramer to be necessary for the spectral changes normally observed on association of the deoxy subunits." @default.
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• W2028762351 date "1972-01-01" @default.
• W2028762351 modified "2023-09-27" @default.
• W2028762351 title "Noncooperativity of the αβ Dimer in the Reaction of Hemoglobin with Oxygen" @default.
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• W2028762351 doi "https://doi.org/10.1073/pnas.69.1.203" @default.
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