title: Pressure acceleration of proteolysis: A general mechanism.
abstract: Remarkable acceleration of enzymatic proteolysis by pressure at kbar range is reported with ubiquitin as substrate and α-chymotrypsin as enzyme. The acceleration is interpreted in terms of the shift of conformational equilibrium in ubiquitin from the non-degradable folded conformer to the enzyme-degradable unfolded conformer by pressure because of the lower volume of the latter, while the enzymatic activity of α-chymotrypsin is still largely retained. This mechanism is considered generally applicable to most globular proteins and the method of pressure-accelerated proteolysis will have an enormous potential utility in systems wherever efficient removal of proteins is needed.
authors.affiliation: High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Akasaka
authors.affiliation: School of Biology-Oriented Science and Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
authors.forename: Harumi
authors.initials: H
authors.lastname: Nagahata
authors.affiliation: School of Biology-Oriented Science and Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
authors.forename: Akihiro
authors.initials: A
authors.lastname: Maeno
authors.affiliation: High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
authors.forename: Ken
authors.initials: K
authors.lastname: Sasaki
keywords: pressure-enhanced proteolysis; shift of conformational equilibrium; ubiquitin; unfolded conformer; α-chymotrypsin