Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 490, Issue 2, Pages 129-136Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2009.08.012
Keywords
Muscle pyruvate kinase; Thermal inactivation; Trehalose; Amyloid-like aggregates; Stability
Categories
Ask authors/readers for more resources
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 degrees C, however, trehalose protects pyruvate kinase from thermal inactivation at 60 degrees C, increases the Tm-app of unfolding by 7.2 degrees 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. (C) 2009 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available