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Articles

Isolation and Preliminary Characterization of a Casein Kinase from Cauliflower Nuclei ¹

Department of Botany, University of Georgia, Athens, Georgia 30610

A casein-type protein kinase has been isolated from cauliflower (Brassica cauliflora Gars.) nuclei and purified to a specific activity of 23,000 units/milligram of protein (1 unit is defined as the transfer of 1 picomole of ³²Pi from -[³²P]ATP to substrate per minute at 28 C). The enzyme has a molecular weight of approximately 39,000 as judged by sucrose density gradient sedimentation. The casein kinase requires ATP as the phosphate donor and will phosphorylate casein and phosvitin, but not histones. The enzyme activity is not affected by cAMP or cGMP. The casein kinase appears to be analogous to casein kinases described in other plant and animal systems.

³ Present address: Department of Botany, University of Minnesota, St. Paul, Minnesota 55108.

¹ This research was supported by National Institutes of Health Grant CA11624.