Isolation and characterization of a new d-galactose-binding lectin from Sambucus racemosa L.
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.
Rojo
M Angeles
MA
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Valladolid, E-47005 Valladolid, Spain.
Citores
Lucía
L
Jiménez
Pilar
P
Ferreras
J Miguel
JM
Arias
F Javier
FJ
Méndez
Enrique
E
Girbés
Tomás
T
D000116:Acetylgalactosamine / Q000378:metabolism; D000595:Amino Acid Sequence; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005690:Galactose / Q000378:metabolism*; D037161:Galectins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry; D054788:Ribosome Inactivating Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D012270:Ribosomes / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D014197:Trees / Q000737:chemistry*
D037161:Galectins; D006023:Glycoproteins; D037121:Plant Lectins; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; C050600:Sambucus nigra lectins; C107391:ebulin r protein, Sambucus ebulus; D054788:Ribosome Inactivating Proteins; D000116:Acetylgalactosamine; D005690:Galactose