Abstract
Summary The conjugate bovine trypsin-dimethylaminonaphtalene-sulfonate is studied by the fluorescence depolarization method. It is shown that the label is heterogeneous but one dansyl residue is strongly bound to the enzyme. After a first fluorescence lifetime determination we found that the trypsin possesses a non-rigid structure. The analysis of the fluorescence decay curve showed us that this decay can be described by a sum of two exponentials. The second order mean decay times gives a higher value for the rotational relaxation time of the protein. The new results are consistent with a rigid structure and between pH 6 and 8 trypsin can be assimilated to a rigid sphere.
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