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Title: Expression of the kinase domain of mouse protein kinase C in E. coli. Author: Dietrich A, Rose-John S, Marks F. Journal: Biochem Int; 1989 Jul; 19(1):163-72. PubMed ID: 2673245. Abstract: The kinase domain of mouse protein kinase C type alpha has been expressed at high levels in E. coli. The protein has been purified 500-fold taking advantage of the fact that highly expressed fusion proteins precipitate out in the bacterial cell and can be solubilized in 7 M urea. The purified protein can be detected with an antibody generated against a PKC alpha derived synthetic peptide. The purified kinase domain exhibits no measurable kinase activity in a protamin phosphorylation assay. This could be an indication that post-translational modifications of the protein kinase domain which do not happen in bacteria are a requirement for functional enzyme activity or that the regulatory domain of protein kinase C is indispensable for kinase function.[Abstract] [Full Text] [Related] [New Search]