Picture of athlete cycling

Open Access research with a real impact on health...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by Strathclyde researchers, including by researchers from the Physical Activity for Health Group based within the School of Psychological Sciences & Health. Research here seeks to better understand how and why physical activity improves health, gain a better understanding of the amount, intensity, and type of physical activity needed for health benefits, and evaluate the effect of interventions to promote physical activity.

Explore open research content by Physical Activity for Health...

Evaluation of cardosin A as a proteolytic probe in the presence of organic solvents

Sarmento, A.C. and Oliveira, C.S. and Pires, E.M. and Halling, P.J. and Barros, M.T. (2004) Evaluation of cardosin A as a proteolytic probe in the presence of organic solvents. Journal of Molecular Catalysis B: Enzymatic, 31 (4-6). pp. 137-141. ISSN 1381-1177

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

Abstract

This investigation showed that cardosin A not only is active in media with organic solvents, cleaving the P-chain of oxidised insulin at three susceptible peptide bonds, but also maintains its specificity in all media tested. Additionally, the presence of organic solvents in the reaction media led to modifications of enzyme selectivity, which enabled the detection of intermediate products. While solvents like ethyl acetate induced a decrease in enzymatic activity, both by reducing the amount of active enzyme and presumably due to an inhibiting effect of ethyl acetate (which might compete with the substrate for the active site of the enzyme), n-hexane caused an increase in the hydrolysis velocity of one peptide bond. In view of the activity and specificity of cardosin A (which shows high preference for hydrophobic residues), it is proposed as a reliable probe for limited proteolysis in the presence of organic solvents. This may become particularly useful for structural characterisation of membrane proteins.