Reactivation of Dark-Inactivated RuBP Carboxylase from Phaseolus vulgaris in vitro

  • J. K. Sainis
  • N. Jawali


It has been proposed that light regulates the activity of RuBP carboxylase by two mechanisms. One is through Activase which has been shown to control the level of carbamylation of enzyme thus controlling the level of activation (1). The other mechanism involves binding of a phosphorylated inhibitor viz 2-carboxy-arabinitol 1-phosphate to the activated form of enzyme at low light intensities and in the dark. Thus after binding with this inhibitor, RuBP carboxylase remains in activated form but is unable to perform catalytic function (2,3,4). This inhibitor along with activase has been shown to match the activity of RuBP carboxylase with RuBP regenerating capacity in vivo (5).


Crude Extract Dependent Activity Bhabha Atomic Research Chloroplastic Protein Multienzyme Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



2-carboxy-D-arabinitol 1-phosphate




Ribulose-1 5-bisphosphate


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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • J. K. Sainis
    • 1
  • N. Jawali
    • 1
  1. 1.Molecular Biology & Agriculture DivisionBhabha Atomic Research CentreTrombay, BombayIndia

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