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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

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Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds

Angela Chambery1 / Anna de Donato2 / Andrea Bolognesi3 / Letizia Polito4 / Fiorenzo Stirpe5 / Augusto Parente6

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Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 9, Pages 1261–1266, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.156, September 2006

Publication History

Received:
March 7, 2006
Accepted:
May 30, 2006
Published Online:
2006-09-14

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: Edman degradation; electrospray dual-ESI-sprayer system; immunotoxin; ribosome-inactivating protein

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[3]
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[7]
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