Physicochemical properties and N-terminal sequence of eel lectin.
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.
D000478:Alkylation; D000595:Amino Acid Sequence; D000818:Animals; D004524:Eels / Q000097:blood*; D007122:Immunoelectrophoresis; D007700:Kinetics; D037102:Lectins; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis
D037102:Lectins; D010446:Peptide Fragments; C027112:fucose-binding lectin