AI Article Synopsis
- Understanding the activity of HTLV-I protease is crucial for developing treatments against HTLV-I infections, but research on this protease has been limited.
- The study successfully produced over 150 mg/L of purified HTLV-I protease and identified optimal cleavage conditions for specific substrates.
- The protease exhibited peak activity at a pH of 5.2-5.3 and 37 degrees Celsius, with no impact from varying sodium chloride concentrations, while key kinetic parameters were evaluated with and without a histidine tag.
Article Abstract
Understanding the factors that affect the activity of Human T-cell Leukemia Virus type I (HTLV-I) protease is essential for the discovery of inhibitors to be used for the treatment of HTLV-I infection, but little has been reported on the protease to date. Here we report the production of HTLV-I protease in purified yields greater than 150 mg/L, determination of its extinction coefficient, and determination of the optimum conditions for cleavage of the p19/24 substrates (DABCYL)-(GABA)-PQVL-Nph-VMH-(EDANS), (DABSYL)-(GABA)-PQVL-Nph-VMH-(EDANS), and (DABSYL)-(GABA)-PQVLPVMH-(EDANS). The highest activity was found at pH 5.2-5.3 and 37 degrees C. There was no effect on activity upon change in sodium chloride concentration from 0 to 1500 mM. The values of K(m) and k(cat) for cleavage of these substrates by the protease with and without the histidine tag were determined.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1006/bioo.2001.1230 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!