Abstract
A lectin has been isolated from the seeds of Lathyrus tingitanus by ammonium sulfate precipitation, affinity chromatography on Sephadex G-100 and subsequent chromatofocusing. This lectin has a relative molecular mass about 50 000 and consists of light ( M r 5000) and heavy subunits ( M r 20 000). The amino acid composition, N-terminal amino acids, carbohydrate and metal content of both the lectin and its subunits are given. This lectin is non-specific in agglutination of human erythrocytes and is inhibited by D-mannose, D-glucose and their α-methylglucosides derivatives. Antibodies against this lectin crossreact with other purified Lathyrus lectins and other lectins from species belonging to the Vicieae tribe.
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