Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942.

@article{Wadano1995PurificationAC,
  title={Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942.},
  author={Akira Wadano and Yayoi Kamata and Toshio Iwaki and Kiyohiro Nishikawa and Tomohiro Hirahashi},
  journal={Plant & cell physiology},
  year={1995},
  volume={36 7},
  pages={1381-5}
}
Phosphoribulokinase (PRK) was purified to electrophoretic homogeneity from Synechococcus PCC7942 with high specific activity. Molecular masses of the native enzyme and its subunit were 178 and 42 kDa, respectively. Cys-17 and Cys-38 were conserved in the cyanobacterial PRK, but 18 amino acid residues between them were missing among the 40 residues found in higher plant PRKs. 

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