Characterization of the binding of the anti-sickling compound, BW12C, to haemoglobin.
The anti-sickling agent BW12C [Beddell, Goodford, Kneen, White, Wilkinson and Wootton (1984) Br. J. Pharmacol. 82, 397-407] was designed to left-shift the oxygen saturation curve of haemoglobin (HbA) by preferential binding to the oxy conformation at a single site between the terminal amino groups of the alpha-chains through Schiff's base formation, ionic and hydrophobic interactions. In the present work, Schiff's base linkages formed with [14C]BW12C were reduced with NaBH4 and the alpha- and...Expand abstract
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