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 53...
| Published in: | Biochemical Journal |
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| Main Author: | |
| Format: | Article in Journal/Newspaper |
| Language: | English |
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Portland Press Ltd.
1984
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1042/bj2200221 https://portlandpress.com/biochemj/article-pdf/220/1/221/580892/bj2200221.pdf |
| Summary: | 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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