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. 1984 May 15;220(1):221–226. doi: 10.1042/bj2200221

Physicochemical properties and N-terminal sequence of eel lectin.

C Kelly
PMCID: PMC1153613  PMID: 6743262

Abstract

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.

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Selected References

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