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- W2000407247 abstract "An adenine phosphoribosyltransferase (E.C. 2.4.2.7) from peach tree (Prunus persica L. Batsch cv. Redhaven) was purified about 600-fold by ammonium sulphate fractionation, DEAE Sephacel and Red Sepha- rose chromatography, and native-PAGE electrophoresis. Polyclonal antibodies were obtained. SDS-PAGE electrophoresis and molecular filtration revealed a single polypeptide of 27.0 ±0.1 kDa. The optimal pH was 8.5. The reaction rate was strictly dependent on the presence of divalent cations, Mn2+ (Km = 48 μmol/L)>Mg2+ (Km = 740 μmol/L)>Cu2+>Ca2+. Kinetic study of the enzyme revealed high specificity and high affinity towards adenine (Km = O.74|umol/L). Among the examined cytokinins, zeatin (Km = 0.30 mmol/L) and benzyladenine were potential substrates. The measured Km towards PRPP was 20 2+mol/L. ADP and AMP only exhibited inhibitory effects: AMP inhibition was competitive towards PRPP (Ki = 25 ± 3 |imol/L). The probable role of the enzyme in recycling adenine and cytokinins is discussed in relation to growth ability acquisition of buds after the release from dormancy." @default.
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- W2000407247 date "1999-03-01" @default.
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- W2000407247 title "Adenine Phosphoribosyltransferase of Peach Tree Leaves: Purification and Properties" @default.
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- W2000407247 doi "https://doi.org/10.1016/s0176-1617(99)80170-9" @default.
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