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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...
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| Główni autorzy: | , , , , , , |
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| Format: | Artigo |
| Język: | Inglês |
| Wydane: |
Public Library of Science
2014
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| Hasła przedmiotowe: | |
| Dostęp online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4177882/ https://ncbi.nlm.nih.gov/pubmed/25255086 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0107932 |
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