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Purification and properties of a lectin from Lathyrus tingitanus seeds
Author(s) -
Rougé Pierre,
Chabert Philippe
Publication year - 1983
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(83)80557-2
Subject(s) - lectin , biochemistry , concanavalin a , ammonium sulfate precipitation , chromatofocusing , lathyrus , agglutination (biology) , chemistry , sephadex , affinity chromatography , molecular mass , amino acid , ammonium sulfate , phytohemagglutinins , ammonium , biology , chromatography , isoelectric point , antibody , size exclusion chromatography , botany , in vitro , immunology , enzyme , immune system , organic chemistry , t cell , lymphocyte activation
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.