Physicochemical properties and N -terminal sequence of eel lectin

• Published in: Biochemical Journal
• Main Author: Kelly, C
• Format: Article in Journal/Newspaper
• Language: English
• Published: Portland Press Ltd. 1984
• Subjects: Cell Biology; Molecular Biology; Biochemistry; Anguilla anguilla
• Online Access: http://dx.doi.org/10.1042/bj2200221; https://portlandpress.com/biochemj/article-pdf/220/1/221/580892/bj2200221.pdf

Some physicochemical properties of the L-fucose-binding lectin from the serum of the European eel (Anguilla anguilla) were determined. The lectin is a dimer composed of identical subunits of Mr approx. 40000. In agreement with previous results [Horejsí & Kocourek (1978) Biochim. Biophys. Acta 538, 299-315], the subunit was shown to comprise two non-glycosylated polypeptides of Mr approx. 20000 and linked by disulphide bonds. N-Terminal sequence analysis, carboxypeptidase digestion and peptide mapping indicated identity of the polypeptides. There were two L-fucose-binding sites per subunit with KD 1.6 X 10(-3) M for the lectin-fucose complex, as determined by equilibrium dialysis.