Stabilization effects of kosmotrope systems on ornithine carbamoyltransferase.
In the present article the influence of salts and additives, such as trehalose, NaCl, ornithine, sodium phosphate and ammonium sulphate, on ornithine carbamoyltransferase (OCTase) is investigated in order to study the OCTase stabilization process as a function of solutes and to point out the fundamental role played by an enhancement of hydrophobic interactions. The synergic use of different techniques, such as neutron spectroscopy, UV-vis spectroscopy, activity and thermal measurements, allows to highlight the cosolute capability to avoid thermal inactivation, to induce important changes in secondary and tertiary enzyme structure and to stabilize biological macromolecules.
Barreca
D
D
Dipartimento di Chimica Organica e Biologica, Università di Messina, P.O. Box 55, S.ta Sperone C.da Papardo, 98166 Messina, Italy.
Bellocco
E
E
Galli
G
G
Laganà
G
G
Leuzzi
U
U
Magazù
S
S
Migliardo
F
F
Galtieri
A
A
Telling
Mark T F
MT
D000818:Animals; D003545:Cysteine; D018940:Elasmobranchii / Q000033:anatomy & histology; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability / Q000187:drug effects; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009954:Ornithine Carbamoyltransferase / Q000737:chemistry* / Q000378:metabolism*; D012492:Salts / Q000494:pharmacology*; D013057:Spectrum Analysis; D013696:Temperature; D013816:Thermodynamics; D017186:Titrimetry
D012492:Salts; D009954:Ornithine Carbamoyltransferase; D003545:Cysteine