4.2 Article

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

Journal

PROTEIN AND PEPTIDE LETTERS
Volume 10, Issue 3, Pages 287-293

Publisher

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/0929866033478979

Keywords

lectin; D-galactose; Sambucus racemosa; ribosome-inactivating protein; bark

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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 mug/ml.

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