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A 1 H NMR comparative study of human adult and fetal hemoglobins
Author(s) -
Yamamoto Yasuhiko,
Nagaoka Tomomi
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00166-5
Subject(s) - tetramer , azide , affinities , hemoglobin , chemistry , bohr effect , fetal hemoglobin , protein subunit , titration , beta (programming language) , amino acid , stereochemistry , crystallography , biochemistry , fetus , biology , genetics , enzyme , pregnancy , inorganic chemistry , organic chemistry , gene , computer science , programming language , oxygen–haemoglobin dissociation curve
The affinities of the individual subunits in human adult and fetal hemoglobins to azide ion have been determined from the combined analysis of NMR and optical titration data. Structural and functional non‐equivalence of the constituent subunits, i.e. α and β subunits in human adult hemoglobin and α and γ subunits in human fetal hemoglobin, has been confirmed. The function of the α subunits, which are common to both hemoglobins, is essentially identical in these hemoglobins and, in spite of the substitutions of 39 amino acid residues between β and γ subunits, they exhibit similar azide ion affinities. The present study also demonstrates that the NMR spectral comparison between the two proteins provides signal assignments to the individual subunits in intact tetramer.