A simple, inexpensive, and sensitive assay for peptidase activity has been devised. The assay was performed in a microtiter plate and was based on fluorogenic peptide substrates, many of which are commercially available. 7-Amino-4-methyl coumarin the fluorescent product liberated during
Activity of cathepsin H,B and metalloproteinase in the serum of patients with acute myocardial infarction.
A László et al.
Clinica chimica acta; international journal of clinical chemistry, 210(3), 233-235 (1992-09-30)
The action of a chymotrypsin-like enzyme from sperm extract from the ascidian Halocynthia roretzi was studied using several substrates. It was found that the most susceptible substrate had the most powerful inhibitory effect on fertilization in this animal. Among the
Frontiers in cardiovascular medicine, 10, 1132786-1132786 (2023-06-02)
Chymase is a highly destructive serine protease rapidly neutralized in the circulation by protease inhibitors. Here we test whether pericardial fluid (PCF) chymase activation and other inflammatory biomarkers determine intensive care unit length of stay, and explore mechanisms of chymase
Previously, MMP-7ases were isolated from rat skeletal muscle by gel filtration and anion exchange chromatography. The enzyme that hydrolyzed succinyl-Ala-Ala-Pro-Phe-AMC (AMC: 7-amino-4-methyl-coumarin) was inhibited by EDTA. In this study we attempted to isolate MMP-7ase from mouse kidney. The isolation procedure
