Akasaka Kazuyuki, Nagahata Harumi, Maeno Akihiro, Sasaki Ken
High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
School of Biology-Oriented Science and Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan.
Biophysics (Nagoya-shi). 2008 Dec 18;4:29-32. doi: 10.2142/biophysics.4.29. eCollection 2008.
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.
据报道，以泛素为底物、α-糜蛋白酶为酶时，在千巴范围内压力可显著加速酶促蛋白水解。这种加速被解释为，由于酶可降解的未折叠构象体体积较小，压力使泛素的构象平衡从不可降解的折叠构象体向酶可降解的未折叠构象体转变，而α-糜蛋白酶的酶活性仍能在很大程度上得以保留。该机制被认为普遍适用于大多数球状蛋白质，并且压力加速蛋白水解的方法在任何需要有效去除蛋白质的系统中都将具有巨大的潜在应用价值。
