Abstract
Two disintegrins were purified from the venom of Crotalus horridus by multiple-dimension liquid chromatography (MDLC) (specifically C18 reverse phase (RP) high-performance liquid chromatography followed by size exclusion chromatography (SEC), and anion exchange chromatography (SCX)). Both disintegrins were subjected to mass spectrometry to determine their intact molecular mass, the number of disulfide linkages, and protein sequence, respectively. These disintegrins were named horrdistatin 1 (nominal mass, 7231 Da) and horrdistatin 2 (nominal mass, 7451 Da), and had IC50(inhibitory concentrations) of 12.5 and 16.2 nmol/L (at 50%), respectively. For sequence confirmation from the C-terminal end, both disintegrins were derivatized using chemical-assisted fragmentation (CAF) and subsequently unzipped via collision-induced dissociation (CID) by matrix-assisted laser desorption ionization quadrupole ion trap time-of-flight (MALDI-QIT-TOF) mass spectrometry.Key words: disintegrins, mass spectrometry, snake venom, Timber rattlesnake, Crotalus horridus.
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