Molecular Adaptation to Physiological Requirements: The Hemoglobin System of Trout
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2014, Food ChemistryCitation Excerpt :Previous work described a pI of 6.2–6.5 for HbIV (Brunori, 1975), which would have enlarged the pH-induced differences in binding of HbIV. For HbI, there was a larger agreement between the pI determination of Brunori (1975) (8.2) and our own (8.4). It can here be mentioned that similar binding behaviour could be expected for other anodic and cathodic fish Hb-components.
Hemoglobin allostery: New views on old players
2013, Journal of Molecular BiologyCitation Excerpt :In HbA, a positively charged cavity, lined by residues His2, Lys82 and His143, is the binding site for DPG and other phosphates.19 In T-HbI, these residues are substituted by Glu2, Leu82 and Ser1439,18; moreover, the conformation of the first three residues of the β subunits (Val1, Glu2 and Trp3) hinders the rim of the pocket on both sides.11 The α1β1 interface, made by residues belonging to the so-called BGH frame from the helices hosting the interacting residues, is quite extensive in both proteins and by-and-large insensitive to the ligation state (Table 1 and Supplementary Tables 1 and 4).
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Present address: Institute of Biochemistry, University of Rome, Rome, Italy.