Lafta, N., Al-Qaisi, A. (2023). Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients. The Egyptian Journal of Hospital Medicine, 90(2), 2574-2580. doi: 10.21608/ejhm.2023.286392
Namariq A. Lafta; Alaa Hussein J. Al-Qaisi. "Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients". The Egyptian Journal of Hospital Medicine, 90, 2, 2023, 2574-2580. doi: 10.21608/ejhm.2023.286392
Lafta, N., Al-Qaisi, A. (2023). 'Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients', The Egyptian Journal of Hospital Medicine, 90(2), pp. 2574-2580. doi: 10.21608/ejhm.2023.286392
Lafta, N., Al-Qaisi, A. Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients. The Egyptian Journal of Hospital Medicine, 2023; 90(2): 2574-2580. doi: 10.21608/ejhm.2023.286392
Inhibition, Characterization and Purification of α-AMY from Sera of Iraqi Breast Cancer Patients
Background: α-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 α-Amylase enzyme, which had been purified from the sera of patients diagnosed with Breast Carcinoma. Materialsand methods: A total of 100 blood serum samples were collected from patients with Breast cancer from Baghdad National Hope Hospital in Baghdad. α-Amylase enzyme was purified from serum clinical isolate in three stages; precipitation with 65% saturated ammonium sulphate, ion exchange chromatography utilizing a DEAE- cellulose 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 α-Amylase enzyme. Results: α-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 non-competitive. 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 α-Amylase purified from sera of Iraqi breast cancer patients was obtained after three purification steps. Ethanolic plant extracts showed inhibitory effect on α-Amylase while Vitis vinifera L. was the most potent inhibitor.
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