Inactivation and Unfolding of Protein Tyrosine Phosphatase from Thermus thermophilus HB27 during Urea and Guanidine Hydrochloride Denaturation

The effects of urea and guanidine hydrochloride (GdnHCl) on the activity, conformation and unfolding process of protein tyrosine phosphatase (PTPase), a thermostable low molecular weight protein from Thermus thermophilus HB27, have been studied. Enzymatic activity assays showed both urea and GdnHCl...

Descripción completa

Detalles Bibliográficos
Autores principales: Wang, Yejing, He, Huawei, Liu, Lina, Gao, Chunyan, Xu, Shui, Zhao, Ping, Xia, Qingyou
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4177882/
https://www.ncbi.nlm.nih.gov/pubmed/25255086
http://dx.doi.org/10.1371/journal.pone.0107932

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4177882/
https://www.ncbi.nlm.nih.gov/pubmed/25255086
http://dx.doi.org/10.1371/journal.pone.0107932

Ejemplares similares