Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin

Figures & data

Table 1. The inhibition profiles of taxifolin on purified hCA I and II from human erythrocytes by sepharose-4B-l-tyrosine-sulfanilamide affinity chromatography and inhibition of AChE purified from electric gel (Electrophorus electricus).

Taxifolin	Kinetic parameters	hCA I	hCA II	AChE
	IC50 (nM)	27.7	43.3	30.1
	R^2	0.9858	0.9682	0.9723
	Ki (nM)	29.2 ± 2.9	24.2 ± 6.5	16.7 ± 3.9
	Inhibition type	Non-competitive	Non-competitive	Non-competitive

Figure 1. Determination of the half maximal inhibitory concentration (IC₅₀) (A) and inhibition constant (K_i) values (B) of taxifolin for human erythrocyte carbonic anhydrase I isoenzyme (hCA I) by using a Lineweaver–Burk graph.

Figure 2. Determination of the half maximal inhibitory concentration (IC₅₀) (A) and inhibition constant (K_i) values (B) of taxifolin for human erythrocyte carbonic anhydrase II isoenzyme (hCA II) by using a Lineweaver–Burk graph.

Figure 3. Determination of the half maximal inhibitory concentration (IC₅₀) value (A) and inhibition constant (K_i) value (B) of taxifolin for acetylcholinesterase enzyme (AChE) by using a Lineweaver–Burk graph.