Binding between thermolysin and its specific inhibitor, N-phosphoryl-L-leucyl-L-tryptophan (PLT).

Abstract

The interaction between thermolysin and its specific inhibitor, PLT (N-phosphoryl-L-leucyl-L-tryptophan), has been investigated by steady-state inhibitory kinetics analysis, fluorometric titration, and the stopped-flow method. The inhibitor constant of PLT, Ki, and the dissociation constant of thermolysin(E)-PLT(I) complex, Kd, are found to be smaller by a… (More)

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Cite this paper

@article{Kitagishi1986BindingBT, title={Binding between thermolysin and its specific inhibitor, N-phosphoryl-L-leucyl-L-tryptophan (PLT).}, author={Keiko Kitagishi and Keitaro Hiromi}, journal={Journal of biochemistry}, year={1986}, volume={99 1}, pages={191-7} }