Kinetic Study of Acetyle CoA Carboxylase-1purified From Serum of Premenopausal Breast Cancer Women

Acetyle CoA Carboxylase-1 was purified from sera of premenopausal women with breast cancer( before Mastectomy or treatment ) by Gel Filtration using Sephadex G-100 and by Ion Exchange using DEAE-Cellulose A-50, also the molecular weight was estimated by the Acrylamide Electrophoresis in the absence...

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Bibliographic Details
Published in:IOP conference series. Materials Science and Engineering 2020-11, Vol.928 (5), p.52026
Main Authors: Mohammad, Sabah G, Ali, Susan J, Saifullah, Perry H
Format: Article
Language:English
Subjects:
Acetyl CoA Carboxylase
Acrylamide
activity
Breast Cancer
Electrophoresis
Gel filtration
Ion exchange
Optimization
purification
Substrates
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Summary:Acetyle CoA Carboxylase-1 was purified from sera of premenopausal women with breast cancer( before Mastectomy or treatment ) by Gel Filtration using Sephadex G-100 and by Ion Exchange using DEAE-Cellulose A-50, also the molecular weight was estimated by the Acrylamide Electrophoresis in the absence of denaturing elements . The result showed that a single band was obtained at 220KD by Gel Filtering while Ion Exchange showed one band at 200KD. The optimum temperature of purified Acetyle CoA Carboxylase-1 was 40 °C, optimal pH at 7.5 and the optimum substrate concentration at 1.8mM. Michaelis-Menten constant (km) was 0.37Mm and Velocity Maximum (Vmax) was 25mM.min−1 The Activation energy(Ea) was 28 KJ/mol.
ISSN:1757-8981
1757-899X
DOI:10.1088/1757-899X/928/5/052026