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来自蜘蛛毒液的多肽神经毒素。

Polypeptide neurotoxins from spider venoms.

作者信息

Grishin E

机构信息

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia.

出版信息

Eur J Biochem. 1999 Sep;264(2):276-80. doi: 10.1046/j.1432-1327.1999.00622.x.

DOI:10.1046/j.1432-1327.1999.00622.x
PMID:10491071
Abstract

Spider venoms contain a variety of toxic components. The polypeptide toxins are divided into low and high molecular mass types. Small polypeptide toxins interacting with cation channels display spatial structure homology. They can affect the functioning of calcium, sodium, or potassium channels. A family of high molecular mass toxic proteins was found in the venom of the spider genus Latrodectus. These neurotoxins, latrotoxins, cause a massive transmitter release from a diversity of nerve endings. The latrotoxins are proteins of about 1000 amino acid residues and share a high level of structure identity. The structural and functional properties of spider polypeptide toxins are reviewed in this paper.

摘要

蜘蛛毒液含有多种有毒成分。多肽毒素分为低分子量型和高分子量型。与阳离子通道相互作用的小多肽毒素表现出空间结构同源性。它们会影响钙、钠或钾通道的功能。在红斑寇蛛属蜘蛛的毒液中发现了一类高分子量有毒蛋白质。这些神经毒素,即黑寡妇蜘蛛毒素,会导致多种神经末梢大量释放神经递质。黑寡妇蜘蛛毒素是由约1000个氨基酸残基组成的蛋白质,具有高度的结构同一性。本文综述了蜘蛛多肽毒素的结构和功能特性。

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