抄録
The aim of this work was to study the selective modification of tryptophan residues with NBS. To accomplish this, a specific method to determine tryptophan was required initially. NBS reacts with both tryptophan and tyrosine residues, which are found in most enzyme proteins, and static spectrophotometric observation, which is usually employed to follow the progress of modification, is not selective for tryptophan. However, discrimination of tryptophan from tyrosine was achieved by the kinetic method with a stopped-flow apparatus. The rate of modification of tryptophan residues is 103 times larger than that of tyrosine, so rapid stop-ping of the reaction of NBS brings about the selective modification of tryptophan residues.
Using fluorescence-spectrophotometric and kinetic methods, the modification with NBS of model compounds of the tryptophan residue could be simply followed as a single phase, even though the reaction is complex when followed by the static spectrophotometric method.
