| dc.creator | Castillo, Jimmy | |
| dc.creator | Hung, Jeanette | |
| dc.creator | Rodríguez, María del C. | |
| dc.creator | Bastidas, Elsy | |
| dc.creator | Laboren, Ivanna | |
| dc.creator | Jaimes, Alba | |
| dc.date | 2017-01-19T16:39:06Z | |
| dc.date | 2017-01-19T16:39:06Z | |
| dc.date | 2005-06-16 | |
| dc.date.accessioned | 2022-10-28T01:20:09Z | |
| dc.date.available | 2022-10-28T01:20:09Z | |
| dc.identifier | Analytical Biochemistry 343 (2005) 293–298 | |
| dc.identifier | 0003-2697 | |
| dc.identifier | http://hdl.handle.net/10872/14054 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4947694 | |
| dc.description | In this work, we report an alternative assay for the determination of the inhibitory eVect on monoamine oxidase B (MAO-B)
activity of probe compounds. Enzyme MAO-B exhibits Xuorescence emissions when it is excited at 412 nm. Using an inexpensive
blue LED-like excitation source, we measured the quenching of Xuorescence intensity of MAO-B enzyme during the reaction with
inhibitors. The applicability of the procedure is demonstrated by assays with L-deprenyl and berberine as inhibitors through the use
of Xuorescence studies. The IC50 values of L-deprenyl and berberine were 0.04 and 90 M, respectively. The KI values were 0.020 and
47 M for L-deprenyl and berberine, respectively. These IC50 and KI values were similar to the values obtained with a standard
method. These results demonstrate the feasibility of this method as an alternative to follow the inhibitory eVect on MAO-B. | |
| dc.language | en_US | |
| dc.publisher | Analytical Biochemistry | |
| dc.subject | MAO-B | |
| dc.subject | LED FLUORESCENCE | |
| dc.subject | BERBERINE | |
| dc.title | LED Xuorescence spectroscopy for direct determination of monoamine oxidase B inactivation | |
| dc.type | Article | |
