Ribonuclease in plant vacuoles: purification and molecular properties of the enzyme from cultured tomato cells

@article{Abel1987RibonucleaseIP,
  title={Ribonuclease in plant vacuoles: purification and molecular properties of the enzyme from cultured tomato cells},
  author={Steffen Abel and Konrad Glund},
  journal={Planta},
  year={1987},
  volume={172},
  pages={71-78}
}
A ribonuclease which was previously shown to be located in isolated vacuoles from suspension-cultured cells of tomato (Lycopersicon esculentum L.; Abel and Glund 1986, Physiol. Plant. 66, 79–86) has been purified to near homogeneity. Purification was up to 55000-fold with a yield of about 20%. The vacuolar origin of the protein was evidenced by comparing its electrophoretic mobility, isoelectric point, pH-optimum for activity and other properties with that of the RNA-degrading activity present… CONTINUE READING

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The molecular weight of the native single polypeptide chain was estimated at 17500 and 20300 by gel filtration and sedimentation analysis , respectively .
The molecular weight of the native single polypeptide chain was estimated at 17500 and 20300 by gel filtration and sedimentation analysis , respectively .
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