Properties and N-terminal amino acid sequences of three Erythrina lectins from Costa Rica (Leguminosae)

 

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Bibliographic Details
Authors: Aragón-Ortiz, Federico, Nanne-Echandi, Clara I, Fink, Edwin
Format: artículo original
Status:Versión publicada
Publication Date:1994
Description:Three Erythrina lectins, from E. fusca, E. globocaliz and E. costaricensis were isolated by affinity chromatography. The lectins are glycoproteins with a monomenc molecular weight of 28 000. They agglutinate human erythrocytes irrespective of blood type and the activity was inhibited by N-acetyl-galactosamine, galactose and lactose. The N-terminal amino acid sequences of the three lectins were deterrnined by automated Edman degradation of the native proteins. Comparison with the sequences of ten other legume lectins revealed extensive homology. The N-terminal amino acid for E.fusca is Val, and Ala for E. globocaliz and E. costaricensis.
Country:Portal de Revistas UCR
Institution:Universidad de Costa Rica
Repositorio:Portal de Revistas UCR
Language:Inglés
OAI Identifier:oai:archivo.portal.ucr.ac.cr:article/23222
Online Access:https://archivo.revistas.ucr.ac.cr/index.php/rbt/article/view/23222