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A glycosylated metallo-protein, nucleotide pyrophosphatase/phosphodiesterase, in a soluble form was purified to homogeneity from prickly pear (Opuntia ficus indica) fruits. The native protein had a molecular mass of 105±8kDa and was formed by two apparently identical subunits each containing 1 Ca 2+ and 1Mg 2+ ion. The Opuntia enzyme exhibited hydrolytic activities toward pyrophosphate/phosphodiester...
An authentic soluble metallo-protein nucleotide pyrophosphatase/phosphodiesterase (ELNPP) was purified to homogeneity from Euphorbia characias latex. The native protein had a molecular mass of 80±5kDa and was shown to be formed by two apparently identical subunits, each containing 1 Ca 2+ and 1 Mg 2+ ion. Whereas Mg 2+ was shown to be strongly bound to the enzyme, Ca 2+...
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