. Author manuscript; available in PMC: 2017 Mar 5.

Published in final edited form as: Eur J Pharmacol. 2016 Feb 3;774:25–33. doi: 10.1016/j.ejphar.2016.01.007

Table 1. Kinetic Parameters, V_max and K_m, for the substrates, MCA-RPGFSAFK-Dnp and 7-Mca-YVADAPK-Dnp, for ACE and ACE2, respectively.

Enzyme	V_max (AFU/min/μg of protein)	K_m (μM)
Recombinant Human ACE2	125 ± 13	23 ± 0.5
Human MNC ACE2	15 ± 4	57 ± 0.6
Murine MNC ACE2	22 ± 6	89 ± 1.9
Recombinant Human ACE	395 ± 70	57 ± 0.8
Human MNC ACE	53 ± 8	68 ± 1.7
Murine MNC ACE	57 ± 14	106 ± 2.7

A representative of time versus substrate hydrolysis curves for each sample shown above is provided in Fig 2. Assays were repeated four times in case of recombinant enzymes or carried out in four different samples in case of human and murine MNCs.

Table 1. Kinetic Parameters, Vmax and Km, for the substrates, MCA-RPGFSAFK-Dnp and 7-Mca-YVADAPK-Dnp, for ACE and ACE2, respectively.

Table 1. Kinetic Parameters, V_max and K_m, for the substrates, MCA-RPGFSAFK-Dnp and 7-Mca-YVADAPK-Dnp, for ACE and ACE2, respectively.