Pimenta A M C, Mansuelle P, Diniz C R, Martin-Eauclaire M F
Laboratoire de Biochimie, Ingénierle des Protéines, UMR 6560, IFR Jean Roche, Bd Pierre Dramard, 13916 Marseille Cedex 20, France.
J Pept Sci. 2003 Feb;9(2):132-40. doi: 10.1002/psc.440.
A toxin with four disulfide bridges from Tityus serrulatus venom was able to compete with 125I-kaliotoxin on rat brain synaptosomal preparations, with an IC50 of 46 nM. The obtained amino acid sequence and molecular mass are identical to the previously described butantoxin. Enzymatic cleavages in the native peptide followed by mass spectrometry peptide mapping analysis were used to determine the disulfide bridge pattern of alpha-KTx12-1. Also, after the cleavage of the first six N-terminal residues, including the unusual disulfide bridge which forms an N-terminus ring, the potency of the cleaved peptide was found to decrease about 100 fold compared with the native protein.
一种来自锯齿蝎毒液的具有四个二硫键的毒素能够在大鼠脑突触体制剂上与125I-卡利毒素竞争，IC50为46 nM。获得的氨基酸序列和分子量与先前描述的布坦毒素相同。通过对天然肽进行酶切，随后进行质谱肽图谱分析，以确定α-KTx12-1的二硫键模式。此外，在切割包括形成N端环的异常二硫键在内的前六个N端残基后，发现切割后的肽的效力与天然蛋白相比降低了约100倍。
