Fig. 5
BIO-A effects on Michaelis-Menten Kinetics of hMAO-A and hMAO-B isozymes: Representative Lineweaver-Burk (LWB) plots of hMAO-A (a) and hMAO-B (b) at their initial velocity (V) with increasing tyramine and benzylamine substrates at RT. c The effects of BIO-A on the parameters of maximum velocity (Vmax) and Michaelis constant (Km) average values in both isozymes. d Following alpha results, inhibitor constant (Ki) was calculated using the competitive model and compared to standard DEP: not applicable (NA) for the competitive model. Data points were expressed as the mean ± SEM, n = 3, representing two experiments. Parameters data are the average of at least two experiments. The significance of the difference between the control and treatments was determined using a one-way ANOVA followed by Dunnett’s multiple comparisons test, or between two groups using unpaired t test. ns: non-significant, *p ≤ 0.05, **p < 0.01, ***p < 0.001