Purification and Characterization of Phosphoribulokinase from the Cyanobacterium Synechococcus PCC7942 |
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| Authors: | Wadano, Akira Kamata, Yoichi Iwaki, Toshio Nishikawa, Keisuke Hirahashi, Tomohiro |
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| Affiliation: | 1 Department of Applied Biochemistry, University of Osaka Prefecture Sakai, Osaka, 593 Japan
2 Department of Veterinary Medicine, University of Osaka Prefecture Sakai, Osaka, 593 Japan |
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| Abstract: | Phosphoribulokinase (PRK) was purified to electrophoretic homogeneityfrom Synechococcus PCC7942 with high specific activity. Molecularmasses of the native enzyme and its subunit were 178 and 42kDa, respectively. Cys-17 and Cys-38 were conserved in the cyanobacterialPRK, but 18 amino acid residues between them were missing amongthe 40 residues found in higher plant PRKs. (Received February 1, 1995; Accepted July 27, 1995) |
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