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Complete structure determination of the A chain of mistletoe lectin III from Viscum album L. ssp. album
Author(s) -
Wacker Roland,
Stoeva Stanka,
Pfüller Karola,
Pfüller Uwe,
Voelter Wolfgang
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.505
Subject(s) - viscum album , lectin , chemistry , botany , biochemistry , biology , traditional medicine , medicine
The complete primary structure of the A chain of mistletoe lectin III (ML3A), a type II ribosome‐inactivating protein, was determined using proteolytic digests of ML3A, HPLC separation of the peptides, Edman degration and MALDI‐MS. Based on our results, ML3A consists of 254 amino acid residues, showing a high homology to the A chain of isolectin ML1 with only 24 amino acid residue exchanges. A striking important structural difference compared with ML1A is the lack of the single N‐glycosylation site in ML3A due to an amino acid exchange at position 112 (ML1A: N 112 GS↠ML3A: T 112 GS). The alignment of ML3A with the A chains of ML1, isoabrins, ricin D, Ricinus communis agglutinin and three lectins, identified from the Korean mistletoe Viscum album ssp. coloratum , demonstrates the rigid conservation of all amino acid residues, responsible for the RNA‐N‐glycosidase activity as reported for ricin D. In addition, the fully determined primary structure of ML3A will give further information about the biological mechanism of mistletoe lectin therapy. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.