Por favor, use este identificador para citar o enlazar este ítem: http://ipicyt.repositorioinstitucional.mx/jspui/handle/1010/1919
Self-association of enolase from Trichomonas vaginalis. monomers, dimers, and octamers coexist in solution
ELIBETH MIRASOL MELENDEZ
ENRIQUE JAIME LIMA MUÑOZ
Víctor Hugo Lara
Luis Gabriel Brieba de Castro
SAMUEL LARA GONZALEZ
CLAUDIA GUADALUPE BENITEZ CARDOZA
Acceso Abierto
Atribución-NoComercial-SinDerivadas
http://dx.doi.org/10.1021/acsomega.8b02197
Plasminogen-binding
Yeast enolase
Triosephosphate isomerase
Streptococcus-pneumoniae
Quaternary structure
Mammalian enolases
Alpha enolase
Protein
Dissociation
Scattering
"We used small-angle X-ray scattering to study the self-association of enolase from Trichomonas vaginalis as a function of the protein concentration and cosolute type. We observed coexisting monomers, dimers, and octamers in variable relative populations, depending on whether Tris–acetate, Tris–HCl, or potassium phosphate buffers were used. Phosphate ions hindered the formation of dimers and octamers. In contrast, the populations of dimers and octamers increased in Tris–acetate or Tris–HCl buffers and additionally increased by augmenting protein concentration or adding magnesium. Single oligomeric species could not be isolated in any of the experimental conditions tested. Furthermore, the secondary and tertiary structures, as well as the temperature-induced denaturation of the mixtures of species, were investigated. The acquired species lost enzymatic activity, but they were prone to interact with plasminogen, as judged from changes in the secondary and tertiary structures upon complex formation."
American Chemical Society
2018
Artículo
ACS Omega 2018, 3, 12, 17871-17880
QUÍMICA
Versión publicada
publishedVersion - Versión publicada
Aparece en las colecciones: Publicaciones Científicas Biología Molecular

Cargar archivos:


Fichero Tamaño Formato  
ACSOmega3(2018)17871.pdf3.94 MBAdobe PDFVisualizar/Abrir