Isolation and characterization of a new d-galactose-binding lectin from Sambucus racemosa L

• Published in: Protein and peptide letters Vol. 10; no. 3; p. 287
• Main Authors: Rojo, M Angeles, Citores, Lucía, Jiménez, Pilar, Ferreras, J Miguel, Arias, F Javier, Méndez, Enrique, Girbés, Tomás
• Format: Journal Article
• Language: English
• Published: Netherlands 01-06-2003
• Subjects: Acetylgalactosamine - metabolism; Amino Acid Sequence; Chromatography, Affinity; Chromatography, Gel; Galactose - metabolism; Galectins - chemistry; Galectins - isolation & purification; Galectins - metabolism; Glycoproteins - chemistry; Molecular Sequence Data; Plant Lectins - chemistry; Plant Proteins - chemistry; Ribosome Inactivating Proteins; Ribosome Inactivating Proteins, Type 2; Ribosomes - enzymology; Sequence Homology, Amino Acid; Trees - chemistry
• ISSN: 0929-8665
• DOI: 10.2174/0929866033478979

A new acidic lectin from red elder (Sambucus racemosa L.) bark has been isolated by affinity chromatography and gel filtration. Noteworthy, and in contrast to other Sambucus species, red elder bark lacks acidic non-toxic type 2 ribosome-inactivating proteins but has basic ribosome-inactivating protein activities. The new lectin (SRLbm) shows specificity for N-Ac-Galactosamine/D-Galactose and has an apparent Mr of 30,000. The N-terminal amino acid sequence displays a close homology with other lectins and B chains of non-toxic type 2 ribosome-inactivating proteins nigrins and ebulins present in other Sambucus species. SRLbm triggers red blood cell agglutination in the range 4-12 micro g/ml.