Related Experiment Videos
Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942
1Department of Applied Biochemistry, University of Osaka Prefecture, Japan.
Plant & Cell Physiology
|October 1, 1995
Abstract:
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.