Investigations of the Inhibition Kinetics of Some Drugs and Chemicals on Enzyme of Polyphenol Oxidase Purified From Apricot's (Salak)
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Date
2007
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Abstract
Polyphenol oxidase (PPO) was purified from Igdir apricot, with a 367 fold purification of PPO by affinity chromatography being achieved. Amount of the protein was determined according to Bradford method. Vmax and Km values were found by means of Lineweaver- Burk graphs. Asetly salisilic acid, paracetamol, ascorbic acid (vitamin C), sodium sulphate, copper sulphate, glucose, sodium nitrite, sodium chlorure, glisine, sodium azide, 2-merkaptoethanol, tyrosine, citric acid, etilendiamin tetra acetic acid (EDTA) ve p-amino benzoic acid were used as inhibitor. Inhibition constants Ki of each inhibitor were found from Lineweaver-Burk graphs. It was found that the p-aminobenzoik acid function showed the highest inhibitory effect.
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Keywords
Characterization, Inhibitor, Kinetics, Polyphenol Oxidase, Purification
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Source
Biosciences Biotechnology Research Asia
Volume
4
Issue
2
Start Page
659
End Page
664