Chemistry of Natural Compounds

, Volume 10, Issue 2, pp 225–226 | Cite as

Isolation and purification of L-asparaginase from Escherichia coli 671

  • R. A. Zhagat
  • D. Ya. Daiya
  • L. V. Poyarkova
  • M. Ya. Orovere
  • A. S. Karsakevich
  • M. A. Geidan
  • G. I. Kleiner
Article
  • 37 Downloads

Conclusions

A modified method for obtaining purified L-asparaginase fromE. coli 671 is proposed. The purification includes extraction with water from an acetone powder, acid-thermal treatment, fractionation with acetone and with polyethyleneglycol, and volume chromatography on DEAE-cellulose.

The specific activity of the L-asparaginase was 200 MU/mg of protein, and the yield of enzyme 19.6%. Its purity was shown by electrophoresis in polyacrylamide gel.

Keywords

Potassium Phosphate Buffer Polyethyleneglycol Cold Acetone Acetone Powder Disk Electrophoresis 

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Copyright information

© Plenum Publishing Corporation 1975

Authors and Affiliations

  • R. A. Zhagat
  • D. Ya. Daiya
  • L. V. Poyarkova
  • M. Ya. Orovere
  • A. S. Karsakevich
  • M. A. Geidan
  • G. I. Kleiner

There are no affiliations available

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