Kucukkilinc_2005_Arch.Biochem.Biophys_440_118

Reference

Title : Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: mechanistic implications - Kucukkilinc_2005_Arch.Biochem.Biophys_440_118
Author(s) : Tuylu Kucukkilinc T , Ozer I
Ref : Archives of Biochemistry & Biophysics , 440 :118 , 2005
Abstract :

The inhibitory effects of the cationic triarylmethane (TAM+) dyes, pararosaniline (PR+), malachite green (MG+), and methyl green (MeG+) on human plasma cholinesterase (BChE) were studied at 25 degrees C in 100 mM Mops, pH 8.0, with butyrylthiocholine as substrate. PR+ and MG+ caused linear mixed inhibition of enzyme activity. The respective inhibitory parameters were K(i) = 1.9 +/- 0.23 microM, alpha = 13 +/- 48, beta = 0 and K(i) = 0.28 +/- 0.037 microM, alpha = 23 +/- 7.4, beta = 0. MeG+ acted as a competitive inhibitor with K(i) = 0.12 +/- 0.017 microM (alpha, infinity, beta, not applicable). The K(i) values were within the same range reported for a number of ChE inhibitors including propidium ion, donepezil, and the phenothiazines, suggesting that TAM+s are active site ligands. On the other hand, the alpha values failed to correlate with values previously reported for a number of ChE inhibitors. It appears that mixed inhibition is the combined result of more than one type of binding and S-I interference. The impact of ligands at the choline-specific and peripheral anionic sites (or, possibly, accessory structural domains) on BChE activity needs to be studied in further detail.

PubMedSearch : Kucukkilinc_2005_Arch.Biochem.Biophys_440_118
PubMedID: 16036213

Related information

Inhibitor Malachite-Green

Citations formats

Tuylu Kucukkilinc T, Ozer I (2005)
Inhibition of human plasma cholinesterase by malachite green and related triarylmethane dyes: mechanistic implications
Archives of Biochemistry & Biophysics 440 :118

Tuylu Kucukkilinc T, Ozer I (2005)
Archives of Biochemistry & Biophysics 440 :118