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The use of nanosecond fluorometry in detecting conformational transitions of an allosteric enzyme
Authors:Ming S. Tung  Robert F. Steiner
Abstract:Analysis of the time decay of fluorescence of 1-anilino-naphthalene-8-sulfonate bound to phosphorylase b reveals the presence of two components with different decay times. In glycylglycine buffer, pH 7.0, the addition of the activators AMP or IMP, or the conversion to phosphorylase a results in a preferential decrease in the amplitude of the component of longer decay time, arising probably from a preferential dissociation of 1-anilino-naphthalene-8-sulfonate from the corresponding site as a consequence of a change in molecular state.
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