Table 4.
Hydrolytic Activity of SAS-1 and SAS-2 toward Caspase and Granzyme B Substrates
Percentage of Z-VAD-AFC
|
|||
---|---|---|---|
Substrate | Protease with Optimal Specificity | SAS-1 | SAS-2 |
Z-VAD-AFCa | Pan-caspase | 100% ± 1.2% | 100% ± 1.9% |
Z-YVAD-AFCa | Caspase-1 | 19% ± 2.1% | 28% ± 2.5% |
Z-VDVAD-AFCa | Caspase-2 | 0% ± 0% | 0% ± 0% |
Z-DEVD-AFCa | Caspase-3 | 0% ± 0% | 0% ± 0% |
Ac-LEVD-AFCa | Caspase-4 | 39% ± 4.4% | 51% ± 2.6% |
Z-WEHD-AFCa | Caspase-5 | 0% ± 0% | 0% ± 0% |
Ac-VEHD-AFCa | Caspase-6 | 311% ± 21.5% | 366% ± 15.6% |
Ac-VEID-AFCa | Caspase-6 | 0% ± 0% | 0% ± 0% |
Ac-VKMD-AFCa | Caspase-6 | 623% ± 32.5% | 654% ± 28.8% |
Ac-VNLD-AFCa | Caspase-6 | 384% ± 18.2% | 521% ± 21.8% |
Ac-IETD-AFCa | Caspase-8 | 130% ± 10.1% | 172% ± 14.7% |
Ac-LEHD-AFCa | Caspase-9 | 105% ± 9.6% | 140% ± 10.2% |
Z-AAD-AFCa | Granzyme B | 144% ± 13.9% | 183% ± 20.1% |
Z-VAD-AFC was used as the 100% control.
Z, benzyloxycarbonyl; Ac, acetyl; AFC, 7-amido-4-(trifluoromethyl)coumarin.
Recognition sequence in single-letter amino acid code.