
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.
Molecular Weight, Autoanalysis, Sequence Analysis, Protein, Molecular Sequence Data, Seeds, Lychnis, Ribosome Inactivating Proteins, Ribosome Inactivating Proteins, Type 1, Amino Acid Sequence, Edman degradation; Electrospray dual-ESI-sprayer system; Immunotoxin; Ribosome-inactivating protein;, Mass Spectrometry
Molecular Weight, Autoanalysis, Sequence Analysis, Protein, Molecular Sequence Data, Seeds, Lychnis, Ribosome Inactivating Proteins, Ribosome Inactivating Proteins, Type 1, Amino Acid Sequence, Edman degradation; Electrospray dual-ESI-sprayer system; Immunotoxin; Ribosome-inactivating protein;, Mass Spectrometry
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