The immunostimulatory activity and stability of grass carp ( Ctenopharyngodon idellus) roe lectin

• Published in: Veterinary Immunology and Immunopathology 2003-08, Vol.94 (3), p.105-112
• Main Authors: Ng, T.B., Lam, Y.W., Woo, N.Y.S.
• Format: Article
• Language: English
• Subjects: Adjuvants, Immunologic - isolation & purification; Adjuvants, Immunologic - metabolism; Adjuvants, Immunologic - pharmacology; Amino Acid Sequence; Animals; Carps - immunology; Carps - metabolism; Chromatography, Affinity - veterinary; Chromatography, Ion Exchange - veterinary; Ctenopharyngodon idella; Ctenopharyngodon idellus; Drug Stability; Freshwater; Grass carp; Hemagglutination - immunology; Hot Temperature; Hydrogen-Ion Concentration; Lectin; Lectins - immunology; Lectins - isolation & purification; Lectins - metabolism; Lectins - pharmacology; Mice; Mice, Inbred ICR; Molecular Sequence Data; Rhamnose - metabolism; Rhamnose-binding; Sea Bream; Sequence Alignment; Sequence Analysis, Protein; Sparus sarba; Spleen - cytology; Spleen - drug effects; Trypsin - metabolism
• ISSN: 0165-2427; 1873-2534; 1365-2567
• DOI: 10.1016/S0165-2427(03)00067-9

A hexameric rhamnose-specific lectin with a molecular mass of 205 kDa and exhibiting some N-terminal sequence similarity to other fish lectins was isolated from roe of the grass carp ( Ctenopharyngodon idellus) by affinity chromatography on rhamnose-Sepharose and ion exchange chromatography by fast protein liquid chromatography on a Mono S column. The lectin exhibited mitogenic activity toward murine splenocytes with a potency lower than that of the plant lectin ConA. It exerted a stimulatory effect at a concentration of 10 μg/ml on the phagocytic activity of seabream ( Sparus sarba) macrophages. It was unstable toward heat (temperature ≥40 °C), acid (0.1 M HCl), alkali (0.1 M NaOH), trypsin and succinylation.