Abstract
The binding of haptoglobin to apohemoglobin (hemoglobin devoid of heme) has been investigated. Haptoglobin of genetic type 1-1 labelled by 1-dimethylamino-naphthalene 5-sulfonyl chloride or 2-dimethylaminonaphthalene 5-sulfonyl chloride has been titrated with apohemoglobin in 20mM phosphate pH 6.8 or 5.7, at 5°C. The formation of the complex has been followed by the increase of the polarization fluorescence. The titration curves show that dansylated haptoglobin and apohemoglobin are in association equilibrium and that one haptoglobin molecule binds two molecules of apohemoglobin. The calculated association constant is K = 4.6 × 10 6.
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