H. Kirschke, E. Shaw
Jul 30, 1981
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0
Influential Citations
79
Citations
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Journal
Biochemical and Biophysical Research Communications
Abstract
Z-Phe-PheCHN/sub 2/ and Z-Phe-AlaCHN/sub 2/ were found to react extremely rapidly with cathepsin L from rat liver lysosomes. For measuring the inactivation time it was necessary to work with dilute enzyme and inhibitor solutions, that is in the range of 10/sup -9/ M. These conditions were made possible through the use of Z-Phe-Arg-4-methyl-7-coumarylamide, a very sensitive substrate suitable for assays of cathepsin L in about 10/sup -12/ M solutions. Z-Phe-AlaCHN/sub 2/ has an affinity for cathepsin L which is about 2000-fold higher than for cathepsin B from rat and human. Z-Phe-PheCHN/sub 2/ proved to be a selective inactivator of cathepsin L in a certain concentration range. Z-Phe-PheCHN/sub 2/ reacts reversibly with cathepsin B from several species.