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- W2428079365 abstract "Seeds of Triticale contain a lectin that agglutinates rabbit erythrocytes whose activity is inhibited by N-Acetylglucosamine and its oligomers. An affinity method has been developed that efficiently binds the lectin activities from Triticale seeds and wheatgerm. Purified Triticale lectin is a glycoprotein with 3% carbohydrate and migrates as a single band corresponding to Mr. 15000 on SDS-PAGE. Antibodies raised to purified wheat germ agglutinin do not cross-react with purified Triticale lectin. Leucine/Isoleucine is the only terminal residue in the Triticale lectin. Presence of inhibitory sugar induces spectral changes in the protein in the UV region. Triticale lectin does not agglutinate human ABO erythrocytes and does not inhibit fungal growth." @default.
- W2428079365 created "2016-06-24" @default.
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- W2428079365 date "1996-04-01" @default.
- W2428079365 modified "2023-09-23" @default.
- W2428079365 title "Affinity purification of N-acetylglucosamine specific lectins. Purification and partial charactersation of triticale lectin." @default.
- W2428079365 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9132153" @default.
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