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...
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Portland Press Ltd.
1984
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crportlandpress:10.1042/bj2200221 2023-05-15T13:27:21+02:00 Physicochemical properties and N -terminal sequence of eel lectin Kelly, C 1984 http://dx.doi.org/10.1042/bj2200221 https://portlandpress.com/biochemj/article-pdf/220/1/221/580892/bj2200221.pdf en eng Portland Press Ltd. Biochemical Journal volume 220, issue 1, page 221-226 ISSN 0264-6021 1470-8728 Cell Biology Molecular Biology Biochemistry journal-article 1984 crportlandpress https://doi.org/10.1042/bj2200221 2022-10-25T16:47:58Z 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. Article in Journal/Newspaper Anguilla anguilla Portland Press (via Crossref) Biochemical Journal 220 1 221 226 |
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Portland Press (via Crossref) |
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English |
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Cell Biology Molecular Biology Biochemistry |
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Cell Biology Molecular Biology Biochemistry Kelly, C Physicochemical properties and N -terminal sequence of eel lectin |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
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. |
format |
Article in Journal/Newspaper |
author |
Kelly, C |
author_facet |
Kelly, C |
author_sort |
Kelly, C |
title |
Physicochemical properties and N -terminal sequence of eel lectin |
title_short |
Physicochemical properties and N -terminal sequence of eel lectin |
title_full |
Physicochemical properties and N -terminal sequence of eel lectin |
title_fullStr |
Physicochemical properties and N -terminal sequence of eel lectin |
title_full_unstemmed |
Physicochemical properties and N -terminal sequence of eel lectin |
title_sort |
physicochemical properties and n -terminal sequence of eel lectin |
publisher |
Portland Press Ltd. |
publishDate |
1984 |
url |
http://dx.doi.org/10.1042/bj2200221 https://portlandpress.com/biochemj/article-pdf/220/1/221/580892/bj2200221.pdf |
genre |
Anguilla anguilla |
genre_facet |
Anguilla anguilla |
op_source |
Biochemical Journal volume 220, issue 1, page 221-226 ISSN 0264-6021 1470-8728 |
op_doi |
https://doi.org/10.1042/bj2200221 |
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Biochemical Journal |
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220 |
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1 |
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221 |
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226 |
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1766397964200181760 |