Erythroagglutinin from Phaseolus coccineus Var. Alubia: Chemical Characterization, Sugar Specificity, and Effect on Blood Coagulation Factors
Por:
Pérez-Campos E., Lascurain R., Sierra C., Espinosa B., Debray H., Bouquelet S., Zenteno E.
Publicada:
1 ene 1997
Resumen:
Purification of the erythroagglutinin from Phaseolus coccineus var. Alubia was achieved by affinity chromatography on human ?1-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 (?1-) 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.
Filiaciones:
Pérez-Campos E.:
Departamento de Bioquímica, Facultad de Medicina, UNAM, 04510, Mexico, Mexico
Lascurain R.:
Departamento de Bioquímica, Inst. Nac. de Enferm. Respiratorias, Mexico D.F., Mexico
Sierra C.:
Laboratorio de Lectinas, Ctro. de Invest. Químicas, Univ. Auton. del Estado de Morelos, Cuernavaca Morelos, Mexico
Espinosa B.:
Ctro. Invest. Biomed. Oriente-IMSS, Puebla, Mexico
Debray H.:
Laboratoire de Chimie Biologique, Univ. des Sci. et Technol. de Lille, 59655 Villeneuve d'Ascq, France
Bouquelet S.:
Laboratoire de Chimie Biologique, Univ. des Sci. et Technol. de Lille, 59655 Villeneuve d'Ascq, France
Zenteno E.:
Departamento de Bioquímica, Facultad de Medicina, UNAM, 04510, Mexico, Mexico
Dep. Bioquímica, Fac. Medicina, UNAM, P.O. Box 70159, 04510 México, Mexico
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