Purification and partial characterization of brain adenosine deaminase: inhibition by purine compounds and by drugs.

@article{Centelles1988PurificationAP,
  title={Purification and partial characterization of brain adenosine deaminase: inhibition by purine compounds and by drugs.},
  author={Josep J. Centelles and Rafael Franco and Jorge Bozal},
  journal={Journal of neuroscience research},
  year={1988},
  volume={19 2},
  pages={258-67}
}
Rat brain adenosine deaminase (E.C. 3.5.4.4.) was purified 667-fold from the supernatant fraction by the following techniques: heat treatment (60 degrees C), fractionation with ammonium sulfate, column chromatography on DEAE-Sepharose, and preparative gel electrophoresis. The purified enzyme was homogeneous by the criterion of polyacrylamide disc gel electrophoresis and isoelectric focusing. Amino acid composition is given. The isoelectric point of the enzyme (5.2) was determined by isoelectric… CONTINUE READING
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