Rhinovirus 3C protease catalyzes efficient cleavage of a fluorescein-labeled peptide affording a rapid and robust assay.
J Biochem Biophys Methods
; 23(2): 107-13, 1991 Sep.
Article
em En
| MEDLINE
| ID: mdl-1658106
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Rhinovirus
/
Proteínas Virais
/
Cisteína Endopeptidases
Idioma:
En
Revista:
J Biochem Biophys Methods
Ano de publicação:
1991
Tipo de documento:
Article