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J. Biol. Chem., Vol. 261, Issue 16, 7115-7118, Jun, 1986

Production of native, correctly folded bovine pancreatic trypsin inhibitor by Escherichia coli

CB Marks, M Vasser, P Ng, W Henzel and S Anderson

A gene for bovine pancreatic trypsin inhibitor (BPTI) was fused to the coding sequence for the Escherichia coli alkaline phosphatase signal peptide and expressed in E. coli under the control of the alkaline phosphatase promoter. When induced in phosphate-depleted medium such cells produced a trypsin inhibitor that was indistinguishable from native, properly folded BPTI. In particular, the BPTI produced by E. coli had three disulfide bonds that appeared to be identical to those found in native BPTI, as assayed by sensitivity to iodoacetate, dithiothreitol, and urea. This expression/secretion system will make possible the production of variant BPTI molecules, thus allowing the perturbing effects of amino acid substitutions on BPTI folding, structure, and function to be assessed.
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				C. Marks, H Naderi, P. Kosen, I. Kuntz, and S Anderson Mutants of bovine pancreatic trypsin inhibitor lacking cysteines 14 and 38 can fold properly Science, March 13, 1987; 235(4794): 1370 - 1373. [Abstract] [PDF]