Abstract
Lipoprotein lipase (LPL) is a key enzyme which regulates the plasma triglyceride concentration by hydrolyzing triglycerides in chylomicrons and very-low-density lipoprotein (VLDL). The activity of LPL was conventionally analyzed using radio-labeled residues or direct sandwich-ELISA. An assay for lipoprotein lipase activity which used a nonradioactive substrate, tri-olein, is described. In this method, LPL activity was detected fluorometrically by reacting 9-anthryldiazomethane (ADAM) with the oleic acid generated from tri-olein by enzyme activity and separated by reversed-phase HPLC. This method has been optimized and the optimum enzyme incubation time and reaction time of the generated oleic acid with ADAM were both at 20 min. The method correlated well with the conventional method.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
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.