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Journal Article

Rapid purification and characterization of protein kinase C from bovine retinal rod outer segments

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Wolbring,  Gregor
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Cook,  Neil J.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Wolbring, G., & Cook, N. J. (1991). Rapid purification and characterization of protein kinase C from bovine retinal rod outer segments. European Journal of Biochemistry, 201(3), 601-606. doi:10.1111/j.1432-1033.1991.tb16320.x.


Cite as: http://hdl.handle.net/21.11116/0000-0007-B2AD-D
Abstract
A rapid FPLC procedure for the purification of protein kinase C from bovine rod outer segments is described. The enzyme is essentially homogeneous after purification and exhibits a molecular mass of approximately 85 kDa, as determined by SDS/PAGE. From its chromatographic behaviour on hydroxyapatite, and from Western-blotting experiments using isoenzyme-specific antibodies, we were able to identify the bovine rod outer segment protein kinase C as being of the alpha or type-III form. The purified protein kinase C has a specific activity of 1066 nmol 32P.min-1.mg protein-1, and shows a 30-fold activation upon the addition of the effectors Ca2+, PtdSer and 1,2-diacylglycerol. Arachidonic acid and linoleic acid were also found to enhance significantly the activity of the purified enzyme.