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, Mn 2+ (Km = 48 μmol/L)>Mg 2+ (Km = 740 μmol/L)>Cu 2+ >Ca 2+ . 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.