Table 5.
Hydrolytic Activity of SAS-1 and SAS-2 toward Various Protease Substrates
| Percentage of Z-VAD-AFC
|
|||
|---|---|---|---|
| Substrate | Protease with Optimal Specificity | SAS-1 | SAS-2 |
| Z-VAD-AFCa | Pan-caspase | 100% ± 2.8% | 100% ± 2.1% |
| Casein | General protease | 0% ± 0% | 0% ± 0% |
| Boc-GGL-pNAa | Subtilisin A | 0% ± 0% | 0% ± 0% |
| A-AAL-pNAa | Subtilisin A | 0% ± 0% | 0% ± 0% |
| SY-AFCa | Dipeptydylpeptidase I | 0% ± 0% | 0% ± 0% |
| GF-AFCa | Dipeptydylpeptidase I | 0% ± 0% | 0% ± 0% |
| PR-AFCa | Dipeptydylpeptidase I | 0% ± 0% | 0% ± 0% |
| GP-AFCa | Dipeptydylpeptidase IV | 0% ± 0% | 0% ± 0% |
| Z-RR-AMCa | Cathepsin B | 0% ± 0% | 0% ± 0% |
| Suc-AAPF-AMCa | Chymotrypsin | 0% ± 0% | 0% ± 0% |
| Z-AKR-AMCa | ICRM Ser protease I | 0% ± 0% | 0% ± 0% |
| H-L-AMCa | Aminopeptidase | 0% ± 0% | 0% ± 0% |
Z-VAD-AFC was used as the 100% control.
Z, benzyloxycarbonyl; Boc, tert-butyloxycarbonyl; Suc, N-succinyl; AFC, 7-amido-4-(trifluoromethyl)coumarin; AMC, 7-amido-4-methylcoumarin.
a
Recognition sequence in single-letter amino acid code.