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Structure of the low molecular weight protein copurified with alpha-latrotoxin.

作者信息

Kiyatkin N, Dulubova I, Chekhovskaya I, Lipkin A, Grishin E

机构信息

Shemyakin Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow.

出版信息

Toxicon. 1992 Jul;30(7):771-4. doi: 10.1016/0041-0101(92)90012-t.

DOI:10.1016/0041-0101(92)90012-t
PMID:1509496
Abstract

Some samples of latrotoxin purified from the black widow spider venom contain two components: alpha-latrotoxin (M(r) approximately 130,000) and a low mol. wt protein with M(r) about 8000. Clones carrying the cDNA sequence for the low mol. wt protein copurified with alpha-latrotoxin were isolated from spider venom glands. Nucleotide sequence analysis of the cloned cDNA revealed the primary structure of the polypeptide to be 18 amino acids signal peptide and 70 amino acids protein chain with mol. wt of 7947 and pI of approximately 4.0. The protein exhibits certain structural homology with erabutoxin-a from the sea snake.

摘要

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Structure of the low molecular weight protein copurified with alpha-latrotoxin.
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The cloning of a cDNA encoding a protein (latrodectin) which co-purifies with the alpha-latrotoxin from the black widow spider Latrodectus tredecimguttatus (Theridiidae).从红斑寇蛛(球腹蛛科)中克隆出一个与α- latrotoxin共纯化的蛋白质(latrodectin)的cDNA。
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Cloning and structure of cDNA encoding alpha-latrotoxin from black widow spider venom.黑寡妇蜘蛛毒液中编码α- Latrotoxin的cDNA的克隆与结构
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