Journal
ANALYTICAL BIOCHEMISTRY
Volume 436, Issue 2, Pages 142-144Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2013.01.031
Keywords
3C protease; Affinity tag removal; Fusion protein protease; Protease; Prescission protease; Tobacco etch virus (TEV) protease
Funding
- Center for Cancer Research, National Cancer Institute, National Institutes of Health
- Hungarian Science and Research Fund [OTKA K101591]
Ask authors/readers for more resources
Because of their stringent sequence specificity, the 3C-like proteases from tobacco etch virus (TEV) and human rhinovirus are often used for the removal of affinity tags. The latter enzyme is rumored to have greater catalytic activity at 4 degrees C, the temperature at which fusion protein substrates are usually digested. Here we report that experiments with fusion protein and peptide substrates confirm this conjecture. Whereas the catalytic efficiency of rhinovirus 3C protease is approximately the same at its optimum temperature (30 degrees C) and at 4 degrees C, TEV protease is 10-fold less active at the latter temperature due primarily to a reduction in k(cat). Published by Elsevier Inc.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available