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. 2022 Jan 28;42(1):BSR20212654. doi: 10.1042/BSR20212654

Table 1. Kinetic parameters of recombinant and natural human LDH.

pH K0.5 (μM) Vmax (nM/s) Hill
Human LDH-A, recombinant
5.0 24.7 ± 3.1 4.1 ± 0.3 1.78 ± 0.27
5.5 43.4 ± 8.7 12.5 ± 2.2 2.32 ± 0.49
6.0 15.7 ± 1.0 24.2 ± 0.8 1.73 ± 0.18
6.5 14.9 ± 0.6 41 ± 1 2.12 ± 0.18
7.0 34.7 ± 1.2 72 ± 1 1.34 ± 0.05
7.5 252 ± 30 276 ± 16 -
8.0 500 ± 44 596 ± 33 -
Human LDH-A, natural
5.0 56 ± 4 19 ± 1 2.01 ± 0.28
5.5 34 ± 3 87 ± 4 1.65 ± 0.19
6.0 43 ± 4 82 ± 4 1.51 ± 0.21
6.5 82 ± 11 211 ± 14 1.13 ± 0.08
7.0 95 ± 9 296 ± 11 -
7.5 210 ± 17 389 ± 15 -
8.0 1083 ± 359 1306 ± 330 -

The Michaelis–Menten or the Hill equation was fitted to the experimental observations shown in Figures 1 and 2. The indicated standard deviations of the enzyme parameters are derived from the fitting of the relevant equation to the experimental observations.