Eduardo Perez-Campos , Ricardo Lascurain, Claudia Sierra, Blanca Espinosa, Henri Debray, Stephane Bouquelet, and Edgar Zenteno.

Laboratorio de Inmunologia, Departamento de Bioquimica, Facultad de Medicina, UNAM, 04510, Mexico; Departamento de Bioquimica, Instituto Nacional de Enfermedades Respiratorias, Mexico D.F.; Laboratorio de Lectinas, Centro de Investigaciones Quimicas, Universidad Autonoma del Estado de Morelos, Cuernavaca Morelos, Mexico; Centro de Investigaciones Biomedicas de Oriente-IMSS, Puebla, Mexico; and Laboratoire de Chimie Biologique (UMR 111 du CNRS), Universite des Sciences et Technologies de Lille, 59655 Villeneuve dasq, France.


Journal of Agricultural and Foof Chemistry. 1997; 45: 3747-3752


Erythroagglutinin from Phaseolus coccineus Var. Alubia: Chemical characterization, sugar specificity, and effect on blood coagulation factors.



Purification of the erythroagglutinin from Phaseolus coccineus var. Alubia was achieved by affinity chromatography on human alfa- acid glycoprotein and by ion exchange chromatography. The lectin is a tetrameric glycoprotein of 31 kDa/subunit with 8% sugar by weight, which agglutinates erythrocytes without serological specificity and is devoid of mitogenic activity toward human peripheral lymphocytes. The specificity of the erythroagglutinin is directed toward the Gal (1-4) or (1-3) GlcNAc (1-2) Man (alfa1-) saccharidic sequence present in bi- or triantennary N-acetyllactosamine- type N-glycopeptides or related glycans. Alubia erythroagglutinin inhibits the generation of human thrombin, very probably by protecting prothrombin from enzymatic cleavage.



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