Mechanical Effects on the Kinetics of the HIV Proteinase Deactivation
| Autor: | Daniel H. Rich, Petr Kuzmic, Anne G. Peranteau, Carlos García-Echeverría |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Chemistry Stereochemistry Hydrolysis Molecular Sequence Data Kinetics Biophysics HIV Protease Inhibitors Cell Biology Biochemistry Catalysis Substrate Specificity Enzyme HIV Protease HIV Protease Inhibitor Amino Acid Sequence Ternary operation Molecular Biology Peptide sequence HIV Proteinase |
| Zdroj: | Biochemical and Biophysical Research Communications. 221:313-317 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1996.0592 |
| Popis: | The proteinase from HIV undergoes rapid and irreversible deactivation caused by mild mechanical stirring. Both the free enzyme and the ternary Michaelis complex disappear in two separate first-order processes, with half-times of 3.0 and 0.8 minutes, respectively. Ignoring these deactivation steps distorts the results of kinetic analyses. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect