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Screening for carbohydrate-binding proteins in extracts of Uruguayan plants 56
Plá,A.; Alonso,E.; Batista-Viera,F.; Franco Fraguas,L..
The presence of carbohydrate-binding proteins, namely lectins, ß-galactosidases and amylases, was determined in aqueous extracts of plants collected in Uruguay. Twenty-six extracts were prepared from 15 Uruguayan plants belonging to 12 Phanerogam families. Among them, 18 extracts caused hemagglutination (HAG) that was inhibited by mono- and disaccharides in 13 cases, indicating the presence of lectins. The other 8 extracts did not cause any HAG with the four systems used to detect HAG activity (rabbit and mouse red cells, trypsin-treated rabbit and mouse red cells). For the extracts prepared from Solanum commersonii, HAG activity and HAG inhibition were similar for those prepared from tubers, leaves and fruits, with the chitocompounds being responsible for...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phanerogam families; Uruguayan plants; Asialofetuin-Sepharose; Carbohydrate-binding proteins; Lectins; SS-Galactosidases; Amylases.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000700005
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Isolation of a ß-galactoside-binding lectin from cat liver 56
Franco-Fraguas,L.; Batista-Viera,F.; Carlsson,J..
A lectin from cat liver has been identified and purified by affinity chromatography on asialofetuin-Sepharose. One hundred micrograms of lectin was obtained from one cat liver with a purification factor of 1561. The lectin agglutinates trypsin-treated rabbit and cow erythrocytes. Hemagglutination was inhibited only by saccharides containing ß-galactosyl residues, of which the 1-amine-1-deoxy-ß-D-galactose was the most potent one by inhibiting hemagglutination at a concentration of 12.5 mM, followed by melibiose, trehalose and galactose. The lectin has a subunit molecular mass of 14.4 kDa determined by SDS-PAGE under reducing conditions and a pI of 4.85. Compared with the composition of lectins from calf heart and porcine heart, cat liver lectin contains...
Tipo: Info:eu-repo/semantics/article Palavras-chave: SS-Galactoside-binding lectin; Galectins; Lectin; Cat liver lectin; Affinity chromatography.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000400005
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