Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942 |
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| Authors: | A Wadano Y Kamata T Iwaki K Nishikawa T Hirahashi |
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| Affiliation: | Department of Applied Biochemistry, University of Osaka Prefecture, Japan. |
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| 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. |
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