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Purification and characterization of Artemia 2′,3′-cyclic nucleotide 3′-phosphodiesterase

AuthorsDíaz, Antonio R.; Heredia, Claudio F.
Issue Date1996
CitationBBA - General Subjects 1290(2): 135-140 (1996)
AbstractThis paper describes the purification and properties of a 2′,3′-cyclic nucleotide 3′-phosphodiesterase which hydrolyzes nucleoside 2′,3′-cyclic monophosphates to nucleoside 2′-phosphates. The enzyme is present in encysted gastrulae of Artemia and its specific activity greatly increases during larval development. The purified enzyme has a molecular weight of around 55 000 as estimated by gel filtration, does not require metals for activity, is inhibited by Zn2+ and inactivated by Cu2+ and has a pH optimum at around neutrality. Based on the relative values of Vmax/Km, the specificity of the phosphodiesterase toward the four 2′,3′-cyclic nucleotides is Guo-2′,3′-P > Ado2′,3′-P > Cyd-2′,3′-P > Urd-2′,3′-P = 45:36:20:7. The enzyme from Artemia gastrulae is competitively inhibited by the four nucleosides 2′-phosphates (Ki values around 1 mM) while the enzyme from larvae is only inhibited by the purine nucleotides. The phosphodiesterase characterized in this work is more similar in substrate specificity to the 2′,3′-cyclic nucleotide 3′-phosphodiesterase from the mammalian nervous system than to the plant enzyme. The functional relationship of this enzyme with the Artemia ribonuclease VI is discussed.
Identifiersdoi: 10.1016/0304-4165(96)00007-4
issn: 0304-4165
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