Abstract
The activity of monoamine oxidase enzymes may be quantified by measuring the conversion of a radiolabeled amine substrate to a radiolabeled product that occurs during incubation of the substrate with the enzyme in an aqueous buffer. Described herein is an established discontinuous procedure in which separation of the substrate and product is achieved by extracting uncharged aldehydes into an organic solvent, while cationic amines remain in an acidified aqueous layer. Under assay conditions designed to ensure a pseudo-linear catalytic rate for the duration of the incubation, determination of radioactivity in the organic solvent by liquid scintillation counting facilitates estimation of an initial rate for amine turnover.
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 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.
