Abstract
Pyruvate ion, which is biologically ubiquitous and participates in many metabolic reactions, was found to be an effective quencher of fluorescence. Compared to other negatively charged quenchers such as I-, pyruvate is not toxic to proteins. By adding an inert, long-lived fluorophore to systems transacting pyruvate, it is possible to estimate activity by measuring the time course of the change in pyruvate quenching of the fluorophore. The procedure is illustrated by measuring the myosin subfragment-1 ATPase activity with a high sensitivity.
| Original language | English |
|---|---|
| Pages (from-to) | 170-175 |
| Number of pages | 6 |
| Journal | Analytical Biochemistry |
| Volume | 129 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1983 Feb 15 |
| Externally published | Yes |
Keywords
- ATPase assay
- charged quencher
- fluorescence quenching
- pyruvate
- pyruvate reactions
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology