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Purification, characterization and 1 H NMR resonance assignment of an α‐like neurotoxin BmK 16 from the venom of chinese scorpion Buthus martensii karsch
Author(s) -
Zhang NaiXia,
Wu Gong,
Wang ZhongHua,
Wu HouMing
Publication year - 2003
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20030211029
Subject(s) - chemistry , edman degradation , scorpion , neurotoxin , venom , peptide sequence , peptide , scorpion toxin , complementary dna , microbiology and biotechnology , biochemistry , gene , biology
A natural scorpion toxin BmK 16 was purified for the first time from the venom of the Chinese scorpion Buthus martensii Karsch (BmK) by using combined gel‐filtration, ion exchange and reversed phase chromatography. The sequence of the N‐ terminal 8 amino acid residues was determined by Edman degradation. Using the TV‐terminal sequence as a tag, the database searching revealed a hit in the scorpion cDNA Bank. The sequence for N‐ terminal 8 amino acid residues, molecular weight and amino acid compositions of BmK 16 were identical with the calculated values according to the first 64 residues′ sequence of the precursor peptide alpha‐neurotoxin TX16 derived from the sequence of the cDNA AF156597 (EMBL). The sequence‐specific resonance assignment of BmK 16 was achieved and the ′intact sequence of BmK 16 was determined as followings: VRDAY IAKPH NCVYE CARNE YCNDL CTKNG AKSGY CQWVG KYGNG CWCKE LPDNV PIRVP GKCH. Furthermore, the results from the sequence homology analysis and the toxicity assays indicated that BmK 16 was an α‐like scorpion neurotoxin.