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. 2019 Oct 9;10:1170. doi: 10.3389/fphar.2019.01170

Table 1.

Kinetic activity of RNase A and the human RNases 1–7.

V0 (µmol/min) B2 ratio
UpA UpG UpI A/G G/I
Bt-RNase A 0.783 ± 0.033 1.49·10−2 ± 9.99·10−4 3.62·10−2 ± 2.22 ·10−3 52.65 0.411
Hs-RNase 1 0.108 ± 3.93·10−3 1.15·10−3 ± 6.09·10−6 7.87·10−3 ± 5.54 ·10−4 93.63 0.146
Hs-RNase 2 2.57·10−3 ± 1.32·10−4 n.d. 5.53·10−4 ± 1.56 ·10−4 0
Hs-RNase 3 2.39·10−3 ± 4.96·10−5 n.d. n.d.
Hs-RNase 4 5.92·10−2 ± 3.97·10−3 2.38·10−3 ± 2.86·10−4 6.86·10−3 ± 1.7 ·10−4 24.85 0.348
Hs-RNase 5 2.39·10−4 ± 3.74·10−5 1.94·10−5 ± 2.5·10−6 5.33·10−5 ± 8.19 ·10−6 12.29 0.365
Hs-RNase 6 6.74·10−3 ± 1.90·10−4 n.d. n.d.
Hs-RNase 7 4.25·10−5 ± 6.21·10−6 n.d. n.d.

The reactions were performed using 100 µM of substrate. Initial velocity (V0) of dinucleotide phosphodiester bond cleavage is indicated. The average of three replicates is shown. Standard error of the mean is shown. n.d.: not detected at the assayed conditions. Bt, Bos taurus; Hs, Homo sapiens.