Protein identification of Trimeresurus macrops venom

Abstract

The protein components from the venom of Trimeresurus macrops have been separated by sodium-dodecyl sulfate polyacrylamide-gel electrophoresis (SDS-PAGE), two-dimensional electrophoresis (2-D electrophoresis), and gel filtration chromatography (GF). The protein profiles SDS-PAGE and 2-D electrophoresis of Trimeresurus macrops venom were obtained. The three molecular masses proteins, which were purified from GF, were determined using matrix assisted laser desorption ionization/time of flight (MALDI/Tof) mass spectrometer; 13732.02 m/z, 13255.68 m/z, and 13341.09 m/z , [M+H]+. The ten amino acids from N-terminal of fraction X protein (13340.09 Da), which was analyzed using Edman degradation, is HVLQLGLYIL The partial sequence of fraction VI protein was determined using electrospray ionization quadrupole/time of flight (ESI-Q/Tof) tandem mass spectrometer. The two product ion spectra of precursor at m /z of 659.3 and 844.3 could be manually interpreted. The first peptide sequence is WAVQCSQQPNR. The second peptide sequence is EAVGEDPWYNHQ(I/L)K. The protein fraction of II and III showed proteolytic activity with specific activity 0.18 and 0.15 unit/ml, respectively. Moreover, the phospholipase A activity was found in the fraction VI protein.