Reciprocal effects in human hemoglobin: direct measurement of the dimer-tetramer association constant at partial oxygen saturation.
نویسندگان
چکیده
منابع مشابه
Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect.
The dimer-tetramer equilibrium constants of human oxyhemoglobin (4K2) and deoxyhemoglobin (0K2) have been determined at 21.5 degrees C as a function of pH and chloride concentration. In buffers containing 0.1 M NaCl, 1 mM EDTA, the apparent numbers of protons released upon assembly of dimers into tetramers were determined from the pH dependencies of 4K2 and 0K2. At pH 7.4, the assembly of unlig...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1978
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.75.11.5493