Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

Reversible acetonitrile-induced inactivation/activation of thermolysin

Ulijn, R.V. and Janssen, A.E.M. and Moore, B.D. and Halling, P.J. and Kelly, S.M. and Price, N.C. (2002) Reversible acetonitrile-induced inactivation/activation of thermolysin. Chembiochem, 3 (11). pp. 1112-1116. ISSN 1439-4227

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

Thermolysin is catalytically inactive in mixtures or 70-15% acetonitrile in aqueous buffer. Unexpectedly, dilution of the inactive enzyme with acetonitrile leads to complete recovery of the catalytic activity in a similar way to dilution with aqueous buffer. Circular dichroism and fluorescence studies of thermolysin in the same solvent mixtures reveal discontinuous changes in the overall secondary and tertiary protein structure that correlate well with the reversible differences in catalytic activity. The spectra on either side of the minimum activity point are different from each other, a fact indicating that the enzyme may be able to access two active conformations which are thermodynamically stable in different solvent environments.