Diffusion-controlled association of a dye, 1-anilinonaphthalene-8-sulfonic acid, to a protein, bovine serum albumin, using a fast-flow microsecond mixer and stopped-flow.
The kinetic constants of the two fastest reactions of 1-anilinonaphthalene-8-sulfonic acid binding to bovine serum albumin are derived from the results of experiments with a microsecond fast-flow mixing technique and a stopped-flow method. The experiments are interpreted in terms of rapid bimolecular diffusion-controlled associations to two independent regions on the protein surface; this reaction mechanism contrasts with previous kinetic studies of ligand binding to bovine serum albumin which have not demonstrated the fastest kinetic processes.
D000817:Anilino Naphthalenesulfonates / Q000032:analysis*; D000818:Animals; D002417:Cattle; D004058:Diffusion; D007700:Kinetics; D012710:Serum Albumin, Bovine / Q000032:analysis*; D013050:Spectrometry, Fluorescence
D000817:Anilino Naphthalenesulfonates; D012710:Serum Albumin, Bovine; C027132:1-anilino-8-naphthalenesulfonate