Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds |
| |
Authors: | Chambery Angela de Donato Anna Bolognesi Andrea Polito Letizia Stirpe Fiorenzo Parente Augusto |
| |
Affiliation: | Dipartimento di Scienze della Vita, Seconda Università di Napoli, Via Vivaldi 43, I-81100 Caserta, Italy. |
| |
Abstract: | The complete amino acid sequence of lychnin, a type 1 ribosome-inactivating protein (RIP) isolated from Lychnis chalcedonica seeds, has been determined by automated Edman degradation and ESI-QTOF mass spectrometry. Lychnin consists of 234 amino acid residues with a molecular mass of 26 131.14 Da. All amino acid residues involved in the formation of the RIP active site (Tyr69, Tyr119, Glu170, Arg173 and Trp203) are fully conserved. Furthermore, a fast MALDI-TOF experiment showed that two out of three cysteinyl residues (Cys32 and Cys115) form a disulfide bridge, while Cys214 is in the thiol form, which makes it suitable for linking carrier molecules to generate immunotoxins and other conjugates. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|