| Autor: |
Hopkins JL; Boehringer Ingelheim Pharmaceuticals Inc., Ridgefield, Connecticut 06877., Betageri R, Cohen KA, Emmanuel MJ, Joseph CR, Bax PM, Pallai PV, Skoog MT |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biochemical and biophysical methods [J Biochem Biophys Methods] 1991 Sep; Vol. 23 (2), pp. 107-13. |
| DOI: |
10.1016/0165-022x(91)90058-5 |
| Abstrakt: |
The 3C protease encoded by human rhinovirus type 2 catalyzes with equal efficiency cleavage of a peptide substrate with or without a fluorescein label attached to the amino acid at the P7' position. Substrates Ac-MEALFQGPLQYKDL-NH2 and MEALFQGPLQYKE(fluorescein)L are hydrolyzed with values of Vmax/KM of 970 M-1 s-1 and 1100 M-1 s-1, respectively. With the labeled substrate, HPLC achieves separation of substrate and product in 2.5 min. Separation in as little as 12 s is feasible. Fluorescein was derivatized so that it could be incorporated into peptides using automated solid-phase peptide synthesis. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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