Purification and Primary
Structure of a Novel Peptide from the Chinese Scorpion Buthus
martensi Karsch
LI Yi-Ming, WU Gong, ZHANG Nai-Xia, WU Hou-Ming*
( Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences,
Shanghai 200032, China )
Abstract 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 C18HPLC, 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.
Key words Buthus martensi Karsch； BmK4112； tandem mass (MS-MS)； CID mass, sequence
determination
*Corresponding author： Tel, 86-21-64163300-1108； Fax, 86-21-64166128； e-mail, [email protected]