Expression and excretion of human pancreatic secretory trypsin inhibitor in lipoprotein-deletion mutant of Escherichia coli |
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Authors: | T Kanamori S Mizushima Y Shimizu H Morishita H Kubota A Nii H Ogino Y Nagase M Kisaragi M Nobuhara |
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Institution: | Research Laboratories for Cell Science, Mochida Pharmaceutical Co., Ltd., Tokyo, Japan. |
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Abstract: | We constructed a gene coding for the 56-amino acid human pancreatic secretory trypsin inhibitor (PSTI), and ligated it on a plasmid downstream from the trp promoter and the signal peptide sequence of alkaline phosphatase. The resulting plasmid was transfected into a lipoprotein deletion mutant (Escherichia coli JE5505) and the plasmid-carrying cells were induced with 3-indoleacrylic acid. A considerable amount (50 micrograms/ml culture) of the mature PSTI protein was detected in the culture supernatant. The excreted PSTI was identical to the natural PSTI protein with respect to the trypsin-inhibiting activity, the N-terminal and the C-terminal amino acid sequences and the amino acid composition. |
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