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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2566| Título : | Kinetics of the thermal inactivation and aggregate formation of rabbit muscle pyruvate kinase in the presence of trehalose |
| Creador: | Guerrero Mendiola C |
| Nivel de acceso: | Open access |
| Palabras clave : | Estabilidad de Enzimas - efectos de drogas - conejos Técnicas In Vitro - métodos - conejos Cinética Músculos -enzimiologia - conejos Conformación Proteica - efectos de drogas - conejos Desnaturalización Proteica - efectos de drogas - conejos Piruvato Quinasa - antagonistas & inhibidores - conejos Piruvato Quinasa - química - conejos Piruvato Quinasa - metabolismo - conejos Espectrometría de Fluorescencia - métodos - conejos Trehalosa - farmacología - conejos Enzyme Stability - drug effects - rabbits In Vitro Techniques methods - rabbits Kinetics Muscles - enzymology - rabbits Protein Conformation - drug effects - rabbits Protein Denaturation - drug effects - rabbits Pyruvate Kinase - antagonists & inhibitors - rabbits Pyruvate Kinase - chemistry - rabbits Pyruvate Kinase - metabolism - rabbits Spectrometry, Fluorescence - methods - rabbits Trehalose - pharmacology - rabbits Amyloid-like aggregates Muscle pyruvate kinase Stability Thermal inactivation Trehalose |
| Descripción : | In a previous study we found that 30-40% dimethylsulfoxide induces the active conformation of rabbit muscle pyruvate kinase. Because dimethylsulfoxide is known to perturb structure and function of many proteins, we have explored the effect of trehalose on the kinetics of thermal inactivation and stability of pyruvate kinase; this is because trehalose, in contrast to dimethyl sulfoxide, is totally excluded from the hydration shell of proteins. The results show that 600 mM trehalose inhibits the activity of pyruvate kinase by about 20% at 25 °C, however, trehalose protects pyruvate kinase from thermal inactivation at 60 °C, increases the Tmapp of unfolding by 7.2 °C, induces a more compact state, and stabilizes its tetrameric structure. The inactivation process is irreversible due to the formation of protein aggregates. Trehalose diminishes the rate of formation of intermediates with propensity to aggregate, but does not affect the extent of aggregation. Remarkably, trehalose affects the aggregation process by inducing aggregates with amyloid-like characteristics. © 2009 Elsevier Inc. All rights reserved. |
| Colaborador(es) u otros Autores: | Oria-Hernández J Ramírez-Silva L |
| Fecha de publicación : | 2009 |
| Tipo de publicación: | Artículo |
| Formato: | |
| Identificador del Recurso : | 10.1016/j.abb.2009.08.012 |
| Fuente: | Archives of Biochemistry and Biophysics 490(2):129 - 136 |
| URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2566 |
| Idioma: | eng |
| Aparece en las colecciones: | Artículos |
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