Abstract
A comparative study was made of the interaction of (2-methoxy-6-chloro-9-acridinyl- N p-aminobenzenearsonate with bovine serum albumin and with specific antibenzearsonate antibodies. The fluorescence increment on binding of the acridine dye to bovine serum albumin was more than 20-fold greater than for the antibodies. Equilibrium dialysis studies, however, showed that two molecules of acridine dye were bound per molecule of bovine serum albumin and of antibody, with close to the same intrinsic equilibrium binding constants in both cases, at pH 9.5 and 25°. Quantitative fluorescence studies of the acridine dye-bovine serum albumin and acridine dye-antibody interactions, as well as fluorescence studies of the dye in nonaqueous solvents, suggest that the acridine dye binds to the two proteins by two quite different mechanisms.
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