Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds.
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.
Chambery
Angela
A
Dipartimento di Scienze della Vita, Seconda Università di Napoli, Via Vivaldi 43, I-81100 Caserta, Italy.
de Donato
Anna
A
Bolognesi
Andrea
A
Polito
Letizia
L
Stirpe
Fiorenzo
F
Parente
Augusto
A
D000595:Amino Acid Sequence; D001322:Autoanalysis / Q000379:methods*; D031244:Lychnis / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D054788:Ribosome Inactivating Proteins / Q000737:chemistry* / Q000302:isolation & purification; D054789:Ribosome Inactivating Proteins, Type 1 / Q000737:chemistry* / Q000302:isolation & purification; D012639:Seeds / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods*
D054789:Ribosome Inactivating Proteins, Type 1; C525537:lychnin; D054788:Ribosome Inactivating Proteins