| Autor: |
BOUHALLAB, S., SAPIN, B., MOLLÉ, D., HENRY, G., LÉONIL, J. |
| Zdroj: |
Journal of Peptide Research; 1997, Vol. 49 Issue 1, p23-27, 5p |
| Abstrakt: |
The sensitivities of the R25-I26 bond on bovine β-casein and on its N-terminal fragment β(1-105) to trypsin digestion were compared by monitoring the liberation of the β(1-25) product. It was shown that this peptide bond was poorly and slowly hydrolysed on β(1-105), while it is highly susceptible to trypsin attack when whole protein is used as substrate. The marked resistance of β(1-105) is linked to its inhibitory effect on trypsin activity (apparent K′i= 1.2 × 10−6, M), as demonstrated by using a related chromogenic substrate. Indeed, a preincubation step of trypsin with β(1-105) leads to a more pronounced inhibitory effect. The progress curves obtained with and without preincubation show that β(1-105) acts as a slow binding inhibitor on trypsin activity. These findings promise further insight into the action and the regulation of proteolytic enzymes. © Munksgaard 1997. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text