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J. Biochem, 1983, Vol. 94, No. 1 129-135
© 1983 Japanese Biochemical Society

research-article

Studies on the Chemical Modification of Tryptophan Residues in Thennolysin and in Talopeptin (MKI) with N-Bromosuccinimide

Keiko KITAGISHI and Keitaro HIROMI

Department of Food Science and Technology, Faculty of Agriculture, Kyoto University Sakyo-ku, Kyoto, Kyoto 606

Tryptophan residues in thermolysin (3 Trp/molecule) and in its specific inhibitor, talopeptin (1 Trp/molecule), were modified with N-bromosuccinimide (NBS). The decrease in the absorption at 280 nm and the fluorescence intensity above 310 nm (excited at 280 nm) accompanying the modification were followed by the stopped-flow method as a function of time. When the sole tryptophan residue of talopeptin was modified with NBS, its inhibitory activity against thermolysin was almost completely destroyed. For thermolysin, the decrease in molar absorptivity corresponds to the modification of one of its three tryptophan residues, and the enzyme activity does not decrease significantly with the modification (remaining activity was 96% at [NBS]/[E] = 6). The results obtained for the modification of El complex suggested that the formation of El complex remarkably reduces the rate constant for the modification of the tryptophan residue in talopeptin, but does not affect that of the tryptophan residue(s) in thermolysin.


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