Abstract
The stopped-flow technique has been applied to the determination of dissociation, phosphorylation, and bimolecular reaction constants for the inhibition of acetylcholinesterase by a potent organophosphate in the presence of a chromogenic substrate. The advantages of the method for inhibition studies are compared with those of an earlier spectrophotometric technique.
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 callDisclaimer: 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.
