Isolation and Purification of Acetylcholine Esterase from the Blood of Breast Cancer Female Patients in Baghdad City

Abstract

Acetylcholinesterase (AChE) breaks down acetylcholine to terminate synaptic transmission, and its regulation influences cancer progression. Blood samples from 20 healthy individuals and 69 breast cancer patients (30 pre- and 39 post-surgery) were analyzed. AChE was purified using techniques like precipitation with [NH₄(SO₄)₂], membrane dialysis, ion-exchange, and gel filtration. The highest enzyme activity (5.9 IU/mg) and yield (65.3%) were obtained by the precipitation with [NH4(SO4)2], while the highest specific activity (0.350 U/mg) was achieved using Sephadex G-100. Optimal enzyme conditions were 34 mM substrate, 28°C, pH 7.6, and 15 minutes incubation time. Kinetics showed Vmax of 5 ng/mL and Km of 20 mM. HPLC yielded 89.3% enzyme purity. Further research is needed to explore AChE's role in cancer.