Inhibition, Characterization and Purification of a-AMY from Sera of Iraqi Breast Cancer Patients.

Background: a-Amylase enzyme is digestive enzyme that breaks down complex carbohydrates like starch into simpler sugars; it is being studied as a potential target for anti-cancer therapies. Objective: The current study aimed to evaluate the general characterization, and inhibition of a-Amylase enzyme, which had been purified from the sera of patients diagnosed with Breast Carcinoma. Materials and Methods: A total of 100 blood serum samples were collected from patients with Breast cancer from Baghdad National Hope Hospital in Baghdad. a-Amylase enzyme was purified from serum clinical isolate in three stages; precipitation with 65% saturated ammonium sulphate, ion exchange chromatography utilizing a DEAEcellulose column, and gel filtration chromatography with a sephadex G-200 column. Changing conditions in pH, temperature, inhibitor concentration, and kinetics all affect the activity of the a-Amylase enzyme. Results: a-Amylase inhibition assay showed that Vitis vinifera L. was the most potent inhibitor (71.8%). During the kinetic investigation of the enzyme, it was discovered that the inhibitory mechanism that the extracts use is noncompetitive. Vmax was 0.023, and 0.012 mmol min -l at 75 µg/ml of Vitis vinifera L., Verbena Officinalis L.extracts, respectively. Conclusions: High specific activity for a-Amylase purified from sera of Iraqi breast cancer patients was obtained after three purification steps. Ethanolic plant extracts showed inhibitory effect on a-Amylase while Vitis vinifera L. was the most potent inhibitor. [ABSTRACT FROM AUTHOR]