Al-Jafari_1995_Toxicology_96_1

Reference

Title : Inhibition of human acetylcholinesterase by cyclophosphamide - Al-Jafari_1995_Toxicology_96_1
Author(s) : Al-Jafari AA , Duhaiman AS , Kamal MA
Ref : Toxicology , 96 :1 , 1995
Abstract :

The inhibitory effect of cyclophosphamide (CP) on human erythrocyte membrane bound acetylcholinesterase (AChE) was investigated in the present study. It was found that CP inhibits the AChE reversibly with an IC50 of 511 microM. The Michaelis-Menten constant (Km) was 132 microM for AChE in the control system; a value increased by 78% in the CP treated system. The Vmax was 73.8 mumol/h/mg protein for the control system. The Lineweaver-Burk plot and Dixon plot indicated that the nature of this inhibition is of the linear mixed type, i.e., partially competitive and purely noncompetitive. The values of Ki and KI were estimated as 378 and 582 microM, respectively. The KI was greater than Ki indicating that noncompetitive inhibition was predominant over competitive.

PubMedSearch : Al-Jafari_1995_Toxicology_96_1
PubMedID: 7863507

Related information

Citations formats

Al-Jafari AA, Duhaiman AS, Kamal MA (1995)
Inhibition of human acetylcholinesterase by cyclophosphamide
Toxicology 96 :1

Al-Jafari AA, Duhaiman AS, Kamal MA (1995)
Toxicology 96 :1