Ornithine Carbamoyltransferase Unfolding States in the Presence of Urea and Guanidine Hydrochloride

Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration...

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Bibliographic Details
Published in:Applied biochemistry and biotechnology 2014, Vol.172 (2), p.854-866
Main Authors: Barreca, D, Lagan , G, Ficarra, S, Tellone, E, Leuzzi, U, Galtieri, A, Bellocco, E
Format: Article
Language:English
Subjects:
additives
Animals
Biochemistry
Biological and medical sciences
Biotechnology
Chemistry
Chemistry and Materials Science
Circular Dichroism
Electrophoresis, Agar Gel
Enzyme Activation - drug effects
Enzymes
Fluorescence
Fundamental and applied biological sciences. Psychology
Guanidine - pharmacology
High temperature
hydrophobicity
Kinetics
ornithine carbamoyltransferase
Ornithine Carbamoyltransferase - metabolism
Protein Folding - drug effects
Protein Structure, Secondary
Sharks
Spectrophotometry, Ultraviolet
Spectrum analysis
temperature
Thermodynamics
ultraviolet-visible spectroscopy
Urea
Urea - pharmacology
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Summary:Ornithine carbamoyltransferase folding/unfolding is a complex and not completely understood process. Our experimental results suggest that ornithine carbamoyltransferase interacts in a completely different way with urea and guanidine hydrochloride. In fact, we noticed that, increasing concentration from 0.0 to 8.0 M of the two additives, the enzyme follows a simple one-step transition mechanism in the presence of guanidine hydrochloride, with two macroscopic states (the native and the denatured one) significantly populated, whereas in the presence of urea a lot of different protein states can be detected and analyzed. Circular dichroism and UV-visible spectroscopy reveal a similar mechanism of perturbation at high temperature, with opening of hydrophobic core and a significant loss in α-helix structure in the presence of guanidine hydrochloride that cannot be found in the presence of urea.
ISSN:0273-2289
1559-0291
DOI:10.1007/s12010-013-0580-9