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J. Biol. Chem., Vol. 266, Issue 17, 10906-10911, Jun, 1991

Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase

J Thomas, SM Van Patten, P Howard, KH Day, RD Mitchell, T Sosnick, J Trewhella, DA Walsh and RA Maurer
Department of Physiology and Biophysics, University of Iowa, Iowa City 52242.

Pure heat-stable inhibitor of the cAMP-dependent protein kinase (PKI) has been isolated in high yield by using a bacterial expression vector constructed to synthesize the complete sequence of the rabbit muscle protein kinase inhibitor, plus an amino-terminal initiator methionine and glycine. Bacterially expressed PKI has an inhibitory activity identical to that of the protein isolated from rabbit skeletal muscle and, by gel filtration and gel electrophoresis, has the same physicochemical characteristics as the native physiological form of PKI. Fourier transformed infrared spectroscopy and CD establish that PKI has unusually large amounts of random coil and turn structures, with significantly smaller amounts of alpha-helix and beta structures.
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