Thermal resistance of pantetheine hydrolase
| Autor: | Raffaella Mancini, Giuseppina Pitari, Giovanni Antonini, Silvestro Duprè |
|---|---|
| Přispěvatelé: | Pitari, G, Antonini, Giovanni, Mancini, R, Dupre, S. |
| Rok vydání: | 1996 |
| Předmět: |
Guanidinium chloride
Protein Denaturation Circular dichroism Swine Kinetics Biophysics GPI-Linked Proteins Kidney Guanidines Biochemistry Amidohydrolases chemistry.chemical_compound Pantetheine hydrolase Structural Biology Enzyme Stability Animals Denaturation (biochemistry) Guanidine Molecular Biology Thermostability chemistry.chemical_classification Chromatography Circular Dichroism Temperature Hydrogen-Ion Concentration Crystallography Enzyme chemistry Isoelectric Focusing |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1298:31-36 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/s0167-4838(96)00112-4 |
| Popis: | Pantetheine hydrolase from pig kidney shows a very high resistance to denaturation with chemical denaturants, being unfolded at concentrations of guanidinium chloride higher than 6.5 M. On the contrary, chemical inactivation, followed by recording catalytic activity, occurs before conformational changes can be detected by fluorimetric or spectroscopic measurements. The enzyme resists temperatures as high as 80 degrees C, as monitored by second derivative spectroscopy and circular dichroism. Activity increases with temperature to an optimum of about 70 degrees C recording the initial velocity. The enzyme behaves very differently against chemical denaturants or against temperature denaturation. These results are unusual for a mesophilic protein. |
| Databáze: | OpenAIRE |
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