Substrate and inhibitor studies of thermolysin-like neutral metalloendopeptidase from kidney membrane fractions. Comparison with bacterial thermolysin
- 1 March 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (6) , 1292-1299
- https://doi.org/10.1021/bi00354a015
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 4 references indexed in Scilit:
- The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11Biochemical Journal, 1984
- Comparison of the structures of carboxypeptidase A and thermolysin.Journal of Biological Chemistry, 1977
- A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substratesJournal of Molecular Biology, 1977
- Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysisBiochemistry, 1977