Abstract
Reaction of bovine trypsinogen with 1-guanyl-3,5-dimethylpyrazole converted all 15 lysine residues to homoarginyl residues. Trypsin could not activate guanidinated trypsinogen but an acid protease from Aspergillus oryzae generated active ∈-guanidinated trypsin by cleaving the Har6–Ile7 bond in the modified zymogen and releasing the activation peptide Val-(Asp)4-Har. After purification by affinity chromatography, the ∈-guanidinated enzyme contained 0.94–0.98 active site/molecule and exhibited the same specific activity toward benzoyl-L-arginine ethyl ester as β-trypsin.
Original language | English (US) |
---|---|
Pages (from-to) | 414-420 |
Number of pages | 7 |
Journal | Biochemistry |
Volume | 12 |
Issue number | 3 |
DOIs | |
State | Published - Jan 1 1973 |
ASJC Scopus subject areas
- Biochemistry