Purification and characterization of glyoxylate synthetase from greening potato-tuber chloroplasts.

@article{Janave1993PurificationAC,
  title={Purification and characterization of glyoxylate synthetase from greening potato-tuber chloroplasts.},
  author={Machhindra T. Janave and Nemmara Krishnan Ramaswamy and P. Madhusudanan Nair},
  journal={European journal of biochemistry},
  year={1993},
  volume={214 3},
  pages={
          889-96
        }
}
Glyoxylate synthetase catalyzing the condensation of two formate molecules into glyoxylate was purified to homogeneity by AcA-34, Sepharose CL-6B and DEAE-Sepharose CL-6B chromatography. A 150-fold purification with a specific activity of 25 mumol . mg protein-1 x 5 min-1 was obtained by this procedure. The reaction product was identified as glyoxylate. The enzyme was a tetramer having a molecular mass of 160 kDa with a subunit molecular mass of 40 kDa. The enzyme could be activated 3-4-fold by… 

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