Fluorescence studies of normal and sickle beta apohemoglobin self-association.

Abstract

The acrylamide quenching of the intrinsic tryptophanyl fluorescence of normal and sickle beta apohemoglobins has been studied in 0.05 M potassium phosphate buffer, pH 7.5, at 5 degrees C over a protein concentration range from 1 to 50 microM. Analysis of quenching dynamics revealed a strong dependence on acrylamide concentration for the intrinsic… (More)

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