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Título : Lectin from Phaseolus acutifolius var. escumite: Chemical characterization, sugar specificity, and effect on human T-lymphocytes
Creador: Castillo Villanueva, Adriana
Nivel de acceso: Open access
Palabras clave : Secuencia de Aminoácidos - fisiología
Carbohidratos - análisis
Carbohidratos - química
División Celular - efectos de drogas
Galactosa - química
humanos
Datos de Secuencia Molecular
Phaseolus - química
Lectinas de Plantas - química
Lectinas de Plantas - metabolismo
Lectinas de Plantas - farmacología
Homología de Secuencia
Linfocitos T - efectos de drogas
Amino Acid Sequence - physiology
Carbohydrates - analysis
Carbohydrates - chemistry
Cell Division - drug effects
Galactose - chemistry
Humans
Molecular Sequence Data
Phaseolus - chemistry
Plant Lectins - chemistry
Plant Lectins - metabolism
Plant Lectins - pharmacology
Sequence Homology
T-Lymphocytes - drug effects
Phaseolus acutifolius var. escumite
lectins
glycoproteins
lectin sugar specificity
mitogenic lectin
Descripción : Purification of the lectin from Phaseolus acutifolius var. escumite was achieved by affinity chromatography on a column containing glutaraldehyzed membranes from blood group O erythrocytes. The lectin is a tetrameric glycoprotein of 121 kDa with 10% of sugar by weight composed by four subunits of 30 kDa as determined by SDS-PAGE. The lectin is composed of four isolectins as determined by ion-exchange chromatography on a mono-S column. The lectin and its isolectins showed identical NH2 terminal residues (ANDLSFNFQR FNETN) with homology to the PHA leucoagglutinin-precursor. Peptide mass fingerprint from each lectin isoform determined from tryptic peptides by MALDI-TOF (matrix assisted laser desorption ionization-time-of-flight) showed differences among subunits, thus suggesting microheterogeneity in their amino acid sequences or different glycosylation patterns. The lectin and its four isolectins agglutinated erythrocytes without serological specificity and showed mitogenic activity on human leukocytes; moreover, the main effect was rather toward CD8+ than to CD4+ human peripheral lymphocytes. The lectin from escumite was not inhibitable by simple sugars; however, the specificity of the lectin and its isoforms was mainly addressed toward galactose residues present in bi- or triantennary N-acetyllactosamine-type glycans
Colaborador(es) u otros Autores: Heriberto Caballero-Ortega
Fikrat Abdullaev-Jafarova
Yonathan Garfias
Maria del Carmen Jiménez-Martínez
Stephane Bouquelet
Gisela Martínez
Guillermo Mendoza-Hernández
Edgar Zenteno
Fecha de publicación : 2007
Tipo de publicación: Artículo
Formato: pdf
Identificador del Recurso : 10.1021/jf063644k
Fuente: Journal of Agricultural and Food Chemistry 55(14):5781 - 5787
URI : http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2575
Idioma: eng
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