The Influence of Phenylalanine on the Enzyme Activity and Fluorescence Emission Intensity of Acid Phosphatase

سال انتشار: 1395
محل انتشار: اولین کنفرانس ملی یافته های نوین زیست شناسی
کد COI اختصاصی: BIOC01_012
زبان مقاله: انگلیسی
تعداد مشاهده: 344

نویسندگان

Postgraduate, MSc in Biochemistry, Shahrekord University

Professor, Shahrekord University

چکیده

Acid phosphatases(APase) EC(3.1.3.2) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7 and optimum temperature of 37 °C. Their function in the production, transmission, and recycling of phosphate is critical for the metabolic and energy transduction processes of the cell. APases belong to a diverse group of binuclear metallohydrolases that use metal ion centers comprising an iron(III) ion and a divalent metal, which is either a zinc(II), manganese(II) or iron(II) ion, to catalyze the hydrolysis of amides and esters of carboxylic and phosphoric acids. The interaction between phenylalanine and APase has been studied by UV-Visible and fluo-rescence spectroscopic measurement. Kinetic studies have been performed using UV-Vis spectrophotometer model: Pharmacia Ultrospect 1100-Pro required with electronic control. Furthermore, fluorometric studies have been performed using UV-Vis spectrofluorometer model: Shimadzu RF-5301PC which requires electronic control .The temperature has been set to 25°C and 35°C for flourometric studies, 37°C for kinetic studies and pH=4.8. The interaction of p-Nitrophenyl phosphate substrate in presence of different concentrations of phenyl-alanine was investigated. The experimental results indicated that by increasing the concentration of this amino acid, the activity of the enzyme enhanced and the fluorescence intensity increased and thus Phenylalanine does.not have the quenching effect on acid phosphatase

کلیدواژه ها

Acid phosphatase, p-Nitrophenyl phosphate, Kinetic, Fluorometry, Quenching, Phenylalanine

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