Spectroscopic characterization of the thermal unfolding of wheat germ agglutinin
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| Format: | Artículo científico |
| Language: | en |
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Sociedad Química de México
2004
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| _version_ | 1876445172379680768 |
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| author | Eneas A. Chavelas |
| author_facet | Eneas A. Chavelas |
| contents | Spectroscopic characterization of the thermal unfolding of wheat germ agglutinin Eneas A. Chavelas Andrea P. Beltrán Gerardo Pérez Hernández Enrique García Hernández Multidisciplinaria (Ciencias Naturales y Exactas) lectin circular dichroism nonobligate homodimer dynamic light scattering We present a study of the thermal unfolding process ofwheat germ agglutinin, a prominent member of the chitin-bindinglectin 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. Thisproperty was confirmed by dynamic light scattering experiments,which revealed that the lectin was monomeric under the conditionsstudied. In literature, wheat germ agglutinin always has been referredto as a homodimer. This is the first time that the agglutinin is revealedas a non-obligate homodimer that dissociates into compact native-likemonomer under acidic conditions. 2004 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47548413 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.4 Vol.48 |
| format | Artículo científico |
| id | redalyc_47548413 |
| institution | Redalyc |
| language | en |
| publishDate | 2004 |
| publisher | Sociedad Química de México |
| spellingShingle | Spectroscopic characterization of the thermal unfolding of wheat germ agglutinin Eneas A. Chavelas Multidisciplinaria (Ciencias Naturales y Exactas) lectin circular dichroism nonobligate homodimer dynamic light scattering Spectroscopic characterization of the thermal unfolding of wheat germ agglutinin Eneas A. Chavelas Andrea P. Beltrán Gerardo Pérez Hernández Enrique García Hernández Multidisciplinaria (Ciencias Naturales y Exactas) lectin circular dichroism nonobligate homodimer dynamic light scattering We present a study of the thermal unfolding process ofwheat germ agglutinin, a prominent member of the chitin-bindinglectin 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. Thisproperty was confirmed by dynamic light scattering experiments,which revealed that the lectin was monomeric under the conditionsstudied. In literature, wheat germ agglutinin always has been referredto as a homodimer. This is the first time that the agglutinin is revealedas a non-obligate homodimer that dissociates into compact native-likemonomer under acidic conditions. 2004 artículo científico 1870-249X https://www.redalyc.org/articulo.oa?id=47548413 en http://www.redalyc.org/revista.oa?id=475 Journal of the Mexican Chemical Society application/pdf Sociedad Química de México Journal of the Mexican Chemical Society (México) Num.4 Vol.48 |
| title | Spectroscopic characterization of the thermal unfolding of wheat germ agglutinin |
| topic | Multidisciplinaria (Ciencias Naturales y Exactas) lectin circular dichroism nonobligate homodimer dynamic light scattering |
| url | https://www.redalyc.org/articulo.oa?id=47548413 |