Hi Everybody, I need to refresh my knowledge a little bit for enzymatic/kinetic assay a little. Current Stopped-flow techniques have been well developed, but some basic concepts of kinetic assay in chemistry should still be the same.
In principle, the catalytic reaction can be stopped by several ways: 1. remove the catalyst. 2. suddenly change the pH of reaction. 3. suddenly dilute the solution into a large quantity. 4. change the reaction temperature: in usual, we like to decrease the temperature from 37(or 25) down to 4 degree C. In usual, the reaction should be slow down. Some papers have reported that enzyme with its intermediate, such as Schiff Base intermediate, can be frozen in the liquid nitrogen by "fresh freezing". Is my concept correct? Thanks. Kevin
