Abstract
An acyl-enzyme intermediate in the catalytic action of the pancreatic serine protease, elastase, was spectrophotometrically observed. 4-Dimethylaminocinnamoyl-elastase was prepared by the reaction of 4-dimethylaminocinnamoylimidazole with a 20 fold excess of elastase for 0.5 hr in pH 5.2 buffer. The visible absorption spectrum of this acyl-enzyme is similar to that of the analogous aldehyde but is red-shifted when compared to that of the denatured acyl-enzyme or a model ester. Our results are the first direct evidence for the intermediacy of an acyl-enzyme in elastase catalysis.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
