The Roles of the Prosequence of Thermolysin in Enzyme Inhibition and Folding in Vitro
Open Access
- 1 October 1996
- journal article
- Published by Elsevier
- Vol. 271 (43) , 26477-26481
- https://doi.org/10.1074/jbc.271.43.26477
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- The Propeptide Is Nonessential for the Expression of Human Cathepsin DPublished by Elsevier ,1995
- The efficiency of processing and secretion of the thermolysin‐like neutral protease from Bacillus cereus does not require the whole prosequence, but does depend on the nature of the amino acid sequence in the region of the cleavage siteMolecular Microbiology, 1994
- Folding of Subtilisin BPN': Role of the Pro-sequenceJournal of Molecular Biology, 1993
- Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragmentBiochemistry, 1993
- A protein-folding reaction under kinetic controlNature, 1992
- The use of a monoclonal antibody for the rapid purification of kidney neutral endopeptidase ("enkephalinase") solubilized in octyl glucosideBiochemistry and Cell Biology, 1987
- The severed activation segment of porcine pancreatic procarboxypeptidase a is a powerful inhibitor of the active enzyme Isolation and characterisation of the activation peptideBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- The adsorption of enkephalin to porous polystyrene beads: A simple assay for enkephalin hydrolysisFEBS Letters, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- On the active site of proteases. III. Mapping the active site of papain; specific peptide inhibitors of papainBiochemical and Biophysical Research Communications, 1968