ISOLATION AND FUNCTION OF A CLOSTRIDIUM-PERFRINGENS ENTEROTOXIN FRAGMENT
ISOLATION AND FUNCTION OF A CLOSTRIDIUM-PERFRINGENS ENTEROTOXIN FRAGMENT
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DOI:
10.1128/iai.55.12.2912-2915.1987
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发表时间:
1987-12-01
影响因子:
3.1
通讯作者:
SAKAGUCHI, G
中科院分区:
文献类型:
--
作者:
HORIGUCHI, Y;AKAI, T;SAKAGUCHI, G
A fragment was obtained by treating Clostridium perfringens enterotoxin with 2-nitro-5-thiocyanobenzoic acid, a reagent which specifically cleaves the amino-terminal peptide bond of cysteine residues. The fragment (molecular weight, 15,000) was purified by high-performance liquid chromatography. The fragment had no cytotoxic effect on Vero cells but competitively inhibited enterotoxin-induced 51Cr release. Binding of 125I-labeled fragment to Vero cells was comparable to that of enterotoxin. Moverover, 125I-labeled fragment did not bind to FL cells, which lack receptor for enterotoxin. We conclude that the fragment contains the binding domain of enterotoxin. The amino acid composition of the fragment suggests that it is located on the carboxyl-terminal part of enterotoxin.