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产气荚膜梭菌ε毒素的色氨酸含量

Tryptophan content of Clostridium perfringens epsilon toxin.

作者信息

Sakurai J, Nagahama M

出版信息

Infect Immun. 1985 Jan;47(1):260-3. doi: 10.1128/iai.47.1.260-263.1985.

DOI:10.1128/iai.47.1.260-263.1985
PMID:2856914
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC261505/
Abstract

The tryptophan content of Clostridium perfringens epsilon toxin was investigated. When the tryptophan content was determined by amino acid analysis after the hydrolysis of epsilon prototoxin with methanesulfonic acid containing 3-(2-aminoethyl)indole and by the spectrophotometric method with N-bromosuccinimide, the number of tryptophan residues was calculated at 1/mol of the protein. Cleavage of the prototoxin or the toxin with N-bromosuccinimide in the presence of urea gave two new fragments on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. There was only a tyrosine residue as the new N-terminal amino acid after the cleavage of the prototoxin or the toxin with N-bromosuccinimide. The data showed that epsilon prototoxin or epsilon toxin contained only one tryptophan residue.

摘要

研究了产气荚膜梭菌ε毒素的色氨酸含量。在用含3-(2-氨基乙基)吲哚的甲磺酸水解ε原毒素后，通过氨基酸分析测定色氨酸含量，并采用N-溴代琥珀酰亚胺分光光度法，计算出蛋白质每摩尔含1个色氨酸残基。在尿素存在下，用N-溴代琥珀酰亚胺切割原毒素或毒素，在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上产生了两个新片段。用N-溴代琥珀酰亚胺切割原毒素或毒素后，仅有一种酪氨酸残基作为新的N端氨基酸。数据表明，ε原毒素或ε毒素仅含有一个色氨酸残基。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4660/261505/ba26dc939a05/iai00118-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4660/261505/ba26dc939a05/iai00118-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4660/261505/ba26dc939a05/iai00118-0277-a.jpg

相似文献

1
Tryptophan content of Clostridium perfringens epsilon toxin.产气荚膜梭菌ε毒素的色氨酸含量
Infect Immun. 1985 Jan;47(1):260-3. doi: 10.1128/iai.47.1.260-263.1985.
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Role of one tryptophan residue in the lethal activity of Clostridium perfringens epsilon toxin.一个色氨酸残基在产气荚膜梭菌ε毒素致死活性中的作用
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Lambda-toxin of Clostridium perfringens activates the precursor of epsilon-toxin by releasing its N- and C-terminal peptides.产气荚膜梭菌的λ毒素通过释放其N端和C端肽段来激活ε毒素的前体。
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Studies on epsilon-prototoxin of Clostridium perfringens type D. Physicochemical and chemical properties of epsilon-prototoxin.产气荚膜梭菌D型ε-原毒素的研究。ε-原毒素的物理化学和化学性质。
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Theta-toxin of Clostridium perfringens. I. Purification and some properties.产气荚膜梭菌的θ毒素。I. 纯化及某些特性
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Conformational studies on modified proteins and peptides. VII. Conformation of epsilon-prototoxin and epsilon-toxin from Clostridium perfringens. Conformational changes associated with toxicity.修饰蛋白质和肽的构象研究。VII. 产气荚膜梭菌ε-原毒素和ε-毒素的构象。与毒性相关的构象变化。
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Amino groups in Clostridium perfringens epsilon prototoxin and epsilon toxin.产气荚膜梭菌ε原毒素和ε毒素中的氨基。
Microb Pathog. 1986 Oct;1(5):417-23. doi: 10.1016/0882-4010(86)90003-3.
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Proteolytic processing and activation of Clostridium perfringens epsilon toxin by caprine small intestinal contents.山羊小肠内容物对产气荚膜梭菌ε毒素的蛋白水解加工与激活
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引用本文的文献

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2
Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coli.产气荚膜梭菌ε毒素基因的克隆、核苷酸测序及其在大肠杆菌中的表达。
Infect Immun. 1992 Jan;60(1):102-10. doi: 10.1128/iai.60.1.102-110.1992.
3
High-affinity binding of Clostridium perfringens epsilon-toxin to rat brain.

本文引用的文献

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Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
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Purification of beta-toxin from Clostridium perfringens type C.从产气荚膜梭菌C型中纯化β毒素
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