Purification and Primary Structure of a Novel Peptide from the Chinese Scorpion Buthus martensi Karsch

To purify and characterize peptides from the venom of Chinese scorpion Buthus martensi Karsch, the purification was carried out by gel-filtration, ion exchange and reversed phase HPLC techniques. The purified peptide was reduced by dithioerythritol (DTT), S-alkylated with iodoacetic acid, and subjected to enzymatic cleavages (TPCK-trypsin). The purified fragments from enzymatic cleavage of the peptide were separated by C(18)HPLC, then submitted to the ESI-MS, and Edman degradation for amino acid sequence determination. The mixture was also subjected to tandem mass (MS-MS) analysis. As a result, a novel peptide, named BmK4112, was obtained, with the primary structure being TPYPV NCKTD RDCVM CGLGI SCKNG YCTGQ C, and having three disulfide bonds.