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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ftpubmed:oai:pubmedcentral.nih.gov:1153613 2023-05-15T13:27:17+02:00 Physicochemical properties and N-terminal sequence of eel lectin. Kelly, C 1984-05-15 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613 http://www.ncbi.nlm.nih.gov/pubmed/6743262 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613 http://www.ncbi.nlm.nih.gov/pubmed/6743262 Research Article Text 1984 ftpubmed 2013-08-30T10:52:55Z 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. Text Anguilla anguilla PubMed Central (PMC) |
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Research Article Kelly, C Physicochemical properties and N-terminal sequence of eel lectin. |
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Research Article |
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 |
Text |
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. |
publishDate |
1984 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613 http://www.ncbi.nlm.nih.gov/pubmed/6743262 |
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Anguilla anguilla |
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Anguilla anguilla |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613 http://www.ncbi.nlm.nih.gov/pubmed/6743262 |
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1766397519143632896 |