| Autor: |
Jodhka, Gurcharan S., Gouda, M. Wafik, Medora, Rustem S., Khalil, Said A. |
| Zdroj: |
Journal of Pharmaceutical Sciences; November 1975, Vol. 64 Issue: 11 p1858-1862, 5p |
| Abstrakt: |
The inhibitory effect of dioctyl sodium sulfosuccinate on the proteolytic activity of trypsin was investigated over the pH 6–8 range. The antitryptic activity was determined using two different substrates: casein and N, α-benzoyl-DL-arginine-p-nitroanilide hydrochloride. The mechanistic studies revealed the substrate-inhibitor interaction to be the overall major mechanism of inhibition. This interaction was shown to involve substrate depletion, probably involving some primary sites of the natural substrate casein. Some inhibition was also shown to be due to an interaction between the enzyme and the inhibitor molecules. The interactions of the inhibitor with the enzyme and the substrate were irreversible. The possible therapeutic significance of the inhibitory effect of the surfactant is discussed. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
Plný text