H. E. Wart, D. Steinbrink
May 15, 1981
Citations
7
Influential Citations
230
Citations
Quality indicators
Journal
Analytical biochemistry
Abstract
Abstract A continuously recording spectrophotometric assay has been developed for Clostridium histolyticum collagenase based on the hydrolysis of 2-furanacryloyl- l -leucylglycyl- l -prolyl- l -alanine (FALGPA). The hydrolysis of this peptide by collagenase obeys Michaelis-Menten kinetics with V = 1.8 × 105μkatal/kg and Km = 0.5 m m . FALGPA is hydrolyzed more rapidly by collagenase than any other commonly used synthetic substrate, but is not cleaved by any of the well-known proteinases such as trypsin, thermolysin, or elastase. The assay itself is rapid, convenient, and sensitive, and should greatly facilitate detailed kinetic studies of collagenase.