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Purification and properties of an N ‐acetylgalactosamine specific lectin from the plant pathogenic fungus Rhizoctonia solani
Author(s) -
Vranken An M.,
Van Damme Els J.M.,
Allen Anthony K.,
Peumans Willy J.
Publication year - 1987
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(87)80758-5
Subject(s) - rhizoctonia solani , lectin , asparagine , biochemistry , mycelium , aspartic acid , glycine , chemistry , affinity chromatography , agglutinin , biology , amino acid , botany , enzyme
A lectin was isolated from Rhizoctonia solani mycelium by affinity chromatography on gum arabic‐Sepharose. It is a dimeric protein composed of 2 identical subunits of 13 kDa with high contents of asparagine/ aspartic acid, valine, glycine, glutamine/glutamic acid and lysine. The R. solani agglutinin (RSA) exhibits specificity towards N ‐acetylgalactosamine, and preferentially agglutinates human type A over type B and type O erythrocytes.