The substrate has the following kinetic constants for βI tryptase: kcat of 17.84 ± 0.40s-1, km of 14.5 ± 1.9 μm, kcat/Km of (1.23 ± 0.15) × 106 s−1 m−1.
The substrate has the following kienetic constants for βII tryptase: kcat of 16.84 ± 0.27s-1, km of 8.9 ± 0.9 μm, kcat/Km of (1.89 ± 0.17) × 106 s−1 m−1.
J.B. Harris, et al., JBC, 276, 34941 (2001).
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