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Protein‐sugar interactions. Purification by affinity chromatography of limulin, an N ‐acyl‐neuraminidyl‐binding protein
Author(s) -
Roche Annie-Claude,
Schauer Roland,
Monsigny Michel
Publication year - 1975
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(75)80309-7
Subject(s) - citation , artificial intelligence , chemistry , library science , computer science
The lectin of Limulus polyphemus haemolymph agglutinates erythrocytes [l-4] and other cells [ 51. Neuraminic acid has been shown to be the specific ligand of this lectin. The lectin has been isolated by ultracentrifugation and preparative starch gel electrophoresis [6], by DEAE-Sephadex and gel filtration chromatography [7] and by ultracentrifugation, affinity and gel filtration chromatography [8]. Though the protein prepared by the last two methods [7,8] was homogeneous with respect to molecular weight, polyacrylamide gel electrophoresis and immunoelectrophoresis, we got three fractions by affinity chromatography. The first two fractions (Limulin I and II) did not agglutinate erythrocytes, but the third fraction (Limulin III) was very active. We wish to report the affinity chromatography purification of Limulin III and to show that Limulin binds O-glycosides of N-acyl-neuraminic acids more strongly than free N-acryl-neuraminic acids.