Abstract
Although various methods have been used to measure the activity of S-adenosyl-l-homocysteine hydrolase (SAHase), most of them are rather complex, expensive, and not suitable for routine analysis. Herein, we describe simple fluorescence monitoring for SAHase activity using a synthetic probe that undergoes chemical binding selectively with l-homocysteine (Hcy), an enzyme metabolite from SAHase catalysis. The ring formation between the probe and Hcy during the enzyme catalysis is quantified by fluorescent emission from the binding adduct, which provides facile, real-time monitoring for the SAHase activity. The chemodosimetric reaction between the probe and Hcy is ∼100-fold faster than that for the enzyme catalysis so that it is successfully applicable in SAHase assay.
| Original language | English |
|---|---|
| Pages (from-to) | 663-668 |
| Number of pages | 6 |
| Journal | Sensors and Actuators, B: Chemical |
| Volume | 185 |
| DOIs | |
| State | Published - 2013 |
Bibliographical note
Funding Information:This work was supported by the Basic Science Research Program, the Pioneer Research Program, and the Bio & Medical Technology Development Program through National Research Foundation of Korea (NRF) grants funded by the Ministry of Education, Science, and Technology (MEST) of South Korea (Grant Nos. 2012-0008314 , 2012-0080734 , and 2012-050100 ).
Keywords
- Chemodosimeter
- Coumarin
- Fluorescent assay
- S-adenosyl-l-homocysteine hydrolase
- l-Homocysteine