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Separation and partial characterization of isolectins with different subunit compositions from Datura stramonium seeds
Author(s) -
Broekaert Willem F.,
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)80887-6
Subject(s) - datura stramonium , protein subunit , lectin , biochemistry , chemistry , glycoprotein , glucosamine , affinity chromatography , sepharose , fetuin , carbohydrate , biology , botany , gene , enzyme
The lectin from Datura stramonium seeds was separated into three individual isolectins by hydrophobic‐interaction chromatography on phenyl‐Sepharose. Two of these isolectins are homodimers made up of two A‐ or two B‐subunits, whereas the third is a heterodimer composed of one A‐ and one B‐subunit. Analysis of the homodimeric AA‐ and BB‐isolectins revealed that the A‐ and B‐subunits have similar but not identical M r values (32 000 and 28 000, respectively), amino acid and carbohydrate compositions. The A‐subunit has a higher affinity for N ‐acetyl‐D‐glucosamine oligomers than the B‐subunit, whereas the latter is more specific for the carbohydrate determinants of some animal glycoproteins such as fetuin, asialofetuin and ovomucoid.