|
ИСТИНА |
Войти в систему Регистрация |
ФНКЦ РР |
||
Mistletoe lectin A-chain unfolds during the intracellular transportстатья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Agapov II, Tonevitsky AG, Maluchenko NV, Moisenovich MM, Kirpichnikov MP
- Журнал: FEBS Letters
- Том: 464
- Номер: 1
- Год издания: 1999
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 63
- Последняя страница: 66
- DOI: 10.1016/S0014-5793(99)01678-6
- Аннотация: Protein conformation during intracellular routing and translocation of the ribosome-inactivating proteins was investigated on hybridomas producing monoclonal antibodies (monAbs) against mistletoe lectin (ML). Decrease in the toxin activity towards these hybridomas is accounted for by the intracellular interaction of monAbs and the toxin resulting in the interruption of enzymatic subunit translocation into the cytosol. Obtained monAbs interacted with denatured ML A-chain (MLA) and a panel of MLA synthetic octapeptides linked to the surface of polyethylene pins. Enzyme-linked immunosorbent assay (ELISA) shows that monAbs recognize five epitopes in denatured MLA. Treatment of MLA by 3 M of guanidine hydrochloride leads to appearance of the epitopes. Hybridoma TA7 has been shown to be insensitive to cytotoxic action of ML. TA7 monAb as we have shown recognizes epitope 101-105, FTGTT, and inhibits the liposome aggregation induced by MLA. A study of the cytotoxicity of ML and ricin for the hybridomas revealed that the unfolding of A-chain is probably required for intracellular transport and cytotoxic activity of ML.
- Добавил в систему: Малюченко Наталия Валериевна