A型肉毒神经毒素纯化及其免疫原性研究

采用阴离子交换柱层析法和凝胶过滤柱层析法纯化A型肉毒神经毒素复合物,通过SDS-PAGE法分析不同纯化条件下目标物的纯度和完整性,并以纯化物免疫BALB/c小鼠研究其免疫原性.结果显示,离子交换柱层析法纯化效果优于凝胶过滤柱层析法.     

东亚钳蝎神经毒素的研究进展

蝎毒中的神经毒素是一类具有特异生物活性的多肽物质。开展对蝎神经毒素的研究是近几年国内外较关注的课题之一。东亚马氏钳蝎（ＢｕｔｈｕｓｍａｒｔｅｎｓｉＫａｒｓｃｈ，ＢｍＫ）是中国分布最广的一种。本文综述了近几年来Ｂｍｋ神经毒素的一级结构研究的一些进展概况     

蝎昆虫神经毒素及其基因研究进展

蝎昆虫神经毒素是一类对昆虫有专一性麻痹致死作用,而对哺乳动物无害或毒性很小的蛋白。因此分离和表达蝎昆虫神经毒素基因,有利于开发研究新型高效生物杀虫剂,并为把该基因导入植物培育新抗虫品种提供必要的基础。另外,此类蝎昆虫神经毒素还有利于研究电压依从性离子通道结构与功能的相互关系。对蝎昆虫神经毒素的研究已成为国内外生物科学工作者关注的课题之一。本文综述了近几年来蝎昆虫神经毒素及其基因的研究进展概况。     

Polyclonal antibody against an insect excitatory toxin BmKIT from Buthus Martensii karsch and detection of BmKIT expressed in transgenic cotton

An insect excitatory toxin gene from Buthus martensii Karseh （BmKIT） was cloned into the expression vector, pET-28a. BmKIT was expressed as inclusion bodies in Eseherichia coli BL21 （DE3） host cells. The authenticity of in vitro expressed protein was confirmed by Western blot. The inclusion body protein band in SDS-PAGE was excised and the protein, BmKIT, was extracted. Polyelonal antibodies to the purified protein were raised in rabbits. The antibody reacted specifically with the expressed BmKIT and was used to quantify its presence in transgenic cotton.     

虎纹捕鸟蛛（Selenocosimia huwena）粗毒对蟾蜍神经肌肉接头传递的影响

１０－５～１０－４ｇ／ｍｌ虎纹捕鸟蛛粗毒对蟾蜍坐骨神经肌肉标本有阻遏作用，１×１０－４ｇ／ｍｌ粗毒发生阻断的时间为３８ｍｉｎ，但不改变神经干动作电位，不影响肌肉对直接刺激的反应。阻断后肌肉对间接强直刺激仍可发生强直收缩；粗毒对蟾蜍坐骨神经肌肉标本的阻断作用表现为：初期４～５０秒的收缩增强继而转向抑制；粗毒可对抗箭毒的阻断作用；蟾蜍在体坐骨神经肌肉标本可被粗毒阻断，但阻断后可以恢复；粗毒不改变蛙腹直肌对Ａｃｈ的敏感性，粗毒中含有拟胆碱成份。箭毒可以阻止粗毒对蛙腹直肌的拟胆碱效应；该粗毒对蟾蜍坐骨神经肌肉标本的阻遏作用发生在神经肌肉接头，粗毒中含有拟胆碱组份，此组份可能通过后膜去极化阻断神经肌肉接头。     

Three-dimensional solution structure of w-conotoxin SO3 determined by ~1H NMR

Cone snails (Conus) elaborate a series of conotoxin (CTX) peptides in their venoms to paralyze their prey. Many of these toxins specifically block ion channels in vertebrate and invertebrate neuromuscular systems[1]. The pattern of Cys residues is quite conserved in most CTXs and can be arranged in three major frameworks: CCCC (a-CTX), CCCCCC (m-CTX), CCCCCC (w-CTX). These peptides have been used as important tools in receptor and ion channel studies[2]. Among these toxins, w-CT…     

Three-dimensional solution structure of ω-conotoxin SO3 determined by^1H NMR

Cone snails (Conus) elaborate a series of conotoxin (CTX) peptides in their venoms to paralyxe their prey.Among these toxins,ω-CTX‘s specifically target to presynaptic voltage-gated calcium channel subsets,causing inhibitlon of neurotransmitter release.ω-CTX SO3 was isolated from the venom of Conus striatus,which is the only available fish-hunting snail solution structure of ω-CTX SO3,a peptide which is the only ω-conotoxin reported to show high homology with another ω-CTX (MVHA from C.Magus),has been determined by ^1H NMR techniques.The molecular structure of ω-CTX SO3 is stabilized by three disulfide bridges and a short triple-stranded antiparallel β-sheet with four turns. A comprehensive comparison suggested that the backbone conformation of ω-CTX‘s was quite conserved,while the length of β-sheet and the type of some turns might have minor differences.