Purification and properties of 5'-nucleotidase from lymphocyte plasma membranes.

@article{Dornand1978PurificationAP,
  title={Purification and properties of 5'-nucleotidase from lymphocyte plasma membranes.},
  author={Jacques Dornand and Jean C Bonnafous and Jean Claude Mani},
  journal={European journal of biochemistry},
  year={1978},
  volume={87 3},
  pages={459-65}
}
5'-Nucleotidase is purified from lymphocyte plasma membranes by two affinity chromatographies. The first one, on Lens culinaris lectin-Sepharose 4B yields a fraction of twelve lectin-binding glycoproteins (lectin-receptor fraction). The second one on 5'-AMP-Sepharose 4B leads to pure enzyme. This enzyme is a glycoprotein with a molecular weight of 130 000; it gives a single band in polyacrylamide/dodecylsulfate electrophoresis and displays a very high specific activity (2500-3000 mumol Pih-1mg… CONTINUE READING