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Revista de la Sociedad Química de México

Print version ISSN 0583-7693


CHAVELAS, Eneas A.; BELTRAN, Andrea P.; PEREZ-HERNANDEZ, Gerardo  and  GARCIA-HERNANDEZ, Enrique. Spectroscopic Characterization of the Thermal Unfolding of Wheat Germ Agglutinin. Rev. Soc. Quím. Méx [online]. 2004, vol.48, n.4, pp.279-282. ISSN 0583-7693.

We present a study of the thermal unfolding process of wheat germ agglutinin, a prominent member of the chitin-binding lectin superfamily. As evidenced by circular dichroism (CD) measurements, the unfolding was fully reversible at acidic conditions, indicating that the process was under thermodynamic control. Thermal CD profiles appeared to be independent on protein concentration, suggesting an unimolecular character for the reaction. This property was confirmed by dynamic light scattering experiments, which revealed that the lectin was monomeric under the conditions studied. In literature, wheat germ agglutinin always has been referred to as a homodimer. This is the first time that the agglutinin is revealed as a non-obligate homodimer that dissociates into compact native-like monomer under acidic conditions.

Keywords : lectin; circular dichroism; dynamic light scattering; non-obligate homodimer.

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