Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)--purification, biochemical properties and behaviour during stress.

@article{Feussner1996Diadenosine5,
  title={Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) hydrolase from tomato (Lycopersicon esculentum cv. Lukullus)--purification, biochemical properties and behaviour during stress.},
  author={Kirstin Feussner and Andrzej Guranowski and Susanne Kostka and Claus Wasternack},
  journal={Zeitschrift fur Naturforschung. C, Journal of biosciences},
  year={1996},
  volume={51 7-8},
  pages={
          477-86
        }
}
Dinucleoside 5',5"'-P1,P4-tetraphosphate hydrolase (EC 3.6.1.17) has been purified to homogeneity from tomato (Lycopersicon esculentum) cells grown in suspension. The purification procedure comprised ammonium sulphate fractionation following five standard chromatography steps and a final chromatography on Ap4A-Sepharose. The homogeneous hydrolase has a molecular mass of 20 kDa and an isoelectric point of 4.5. The enzyme hydrolyses diadenosine tetraphosphate (Ap4A) asymmetrically to AMP and ATP… CONTINUE READING

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