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...

Full description

Bibliographic Details
Main Author: Kelly, C
Format: Text
Language:English
Published: 1984
Subjects:
Research Article
Anguilla anguilla
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613
http://www.ncbi.nlm.nih.gov/pubmed/6743262
id ftpubmed:oai:pubmedcentral.nih.gov:1153613
record_format openpolar
spelling 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)
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Research Article
spellingShingle Research Article
Kelly, C
Physicochemical properties and N-terminal sequence of eel lectin.
topic_facet 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
genre Anguilla anguilla
genre_facet Anguilla anguilla
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1153613
http://www.ncbi.nlm.nih.gov/pubmed/6743262
_version_ 1766397519143632896

Similar Items