NMR in interaction studies of a serine protease from snake venom

Abstract

In this research, we have purified a serine protease from Bothrops jararaca venom (BjSP24). This enzyme showed molar mass of 24.4 kDa as determined using MALDI-TOF. BjSP24 inhibition by hesperitin (Hst) was studied using florescence, enzymatic kinetics and nuclear magnetic resonance techinique (Saturation Transferee Difference, STD-NMR).