, Volume 157, Issue 3, pp 245–253 | Cite as

Purification and properties of two forms of glutamine synthetase from the plant fraction of Phaseolus root nodules

  • Julie V. Cullimore
  • M. Lara
  • P. J. Lea
  • B. J. Miflin


Two forms of glutamine synthetase (GS) have been purified to apparent homogeneity from the plant fraction of Phaseolus vulgaris root nodules. One of these forms appears identical to the form of the enzyme found in roots but the other is probably specifically associated with the nodule. Free-living Rhizobium phaseoli also contain two forms of GS both of which have different molecular weights from the plant enzymes. Bacteroids contain solely the higher-molecular-weight form of rhizobial GS. There are only minor differences between the plant enzymes in Km or S0.5 values for the synthetase-reaction substrates and both forms have identical molecular weights of the holoenzyme (380,000 daltons) and its sub-units (41,000 daltons). They can be separated by ion-exchange chromatography on diethylaminoethyl-Sephacel and by native polyacrylamide-gel electrophoresis. The only other distinguishing feature observed is that the ratio of transferase: synthetase activity of the root form is threefold greater than that of the nodule-specific GS.

Key words

Glutamine synthetase Legume Rhizobium symbiosis Nitrogen assimilation Phaseolus (glutamine synthetase) Rhizobium Root nodule 





glutamine synthetase


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Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • Julie V. Cullimore
    • 1
  • M. Lara
    • 1
  • P. J. Lea
    • 1
  • B. J. Miflin
    • 1
  1. 1.Biochemistry DepartmentRothamsted Experimental StationHarpendenUK

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