Isolation and partial characterization of a small chitin‐binding lectin from mistletoe (Viscum album)

FEBS Letters

Verhaert, Peter²  Pfüller, Uwe¹  Peumans, Willy J.³  Van Damme, Els J.M.³ 

[1] Institut für Phytochemie, University of Witten, Stockumerstrasse 10, 58448 Witten, Germany;Laboratorium voor Ontwikkelingsfysiologie en Moleculaire Biologie, Katholieke Universiteit Leuven, Naamsestraat 59, 3000 Leuven, Belgium;Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, 3001 Leuven, Belgium

关键词: Viscum album;    Mistletoe;    Lectin;    Cytotoxicity;    Chitin binding;    MALDI-TOF;    matrix-assisted laser desorption ionization time of flight;    ML;    mistletoe lectin;    MS;    mass spectrometry;    PBS;    phosphate-buffered saline (1.5 mM KH2PO4;    10 mM Na2HPO4;    3 mM KCl;    140 mM NaCl;    pH 7.4);    RIP;    ribosome-inactivating protein;    SDS-PAGE;    sodium dodecyl sulphate-polyacrylamide gel electrophoresis;    VisalbCBA;    Viscum album chitin-binding agglutinin;   

DOI  :  10.1016/0014-5793(96)01108-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel lectin, called VisalbCBA, was isolated from European mistletoe (Viscum album). This lectin differs completely from the classical galactose/N-acetylgalactosamine-binding mistletoe lectins MLI, MLII and MLIII. Biochemical analyses indicated that VisalbCBA is a dimeric protein composed of two identical subunits of approx. 10 kDa. VisalbCBA exhibits specificity towards oligomers of N-acetylglucosamine and shows sequence homology to the previously isolated chitin-binding plant proteins. Although VisalbCBA is less toxic than the other mistletoe lectins, it definitely exhibits cytotoxic properties. The possible involvement of VisalbCBA in the biological and therapeutic effects of mistletoe is discussed.

【 授权许可】

Unknown