Fig. 4: Stability of ultraphosphates in aqueous media and enzymatic digestion.
a Decomposition of trisadenosine ultraphosphate (21) and uP4 under different pH values and in presence of 0.1 eq. of different cations. Half-lives were calculated assuming pseudo-first-order reaction kinetics. b Enzymatic digestion of tris(para-nitrophenyl) ultraphosphate (31) by alkaline phosphatase (ALP) from bovine intestinal mucosa. Kinetics were recorded using 31P{1H}-NMR and the [PPN] signal was used as an internal standard. The results are means ± standard deviation from experiments performed in triplicates. Half-lives were calculated assuming pseudo-first-order reaction kinetics. I, 31 in the presence (green) and absence (black) of ALP. II, 31 with 20 mm EDTA in the presence (blue) and absence (black) of ALP. III, 31 in the presence (red) and absence (black) of heat-inactivated ALP. c Decomposition of tris(para-nitrobenzyl phosphonyl) ultraphosphate (63).
