The cDNA encoding a novel isoform of human trypsinogen was identified. The isoelectric points of the proenzyme and active forms calculated from the deduced amino acid sequence are consistent with those of mesotrypsin(ogen), known to be an inhibitor-resistant trypsin isoform. The cDNA attached with a bacterial signal peptide sequence was expressed in Escherichia coli. The recombinant proenzyme p...

The effect of 3 purified trypsin inhibitors and 4 legume seed extracts on teh trypsins and chymotrypsins of the activated pancreata of 11 animal species, including man, was measured. The activation was performed by either homologous enterokinase or by bovine trypsin. Several trypsinogens were not activated by the latter. Rabbit trypsin was the most sensitive to all inhibitor preparations, while...

I R TERRY, D A W GRAN , AND .1 111ERMONTAY L.OR (Depaoritnew of0 KSurgeriv, St Geotrge's Hospitall, Lon1doni) Appropriate intraperitoncal antiproteinase chemotherapy for ANP may include the use of oligopeptide inhibitors of bacterial origin as these agents are capable of inactivating pancreatic proteinases of different specificities in compilex with (xL-maicroglobulin.' We h.lve studied the eft...

We have developed a high throughput assay for the measurement of protease activity in solution. This technology will accelerate research in functional proteomics and enable biologists to streamline protease substrate evaluation and optimization. The peptide sequences that serve as protease substrates in this assay are labeled on the carboxy terminus with a biotin moiety and a fluorescent tag is...

The third domain of the periplasmic protein TolA from Escherichia coli (TolAIII) was used as a fusion partner in the expression of various proteins from bacteria and eukaryotes. TolAIII is small domain, expressed in high yields as a soluble protein in the cytoplasm of E. coli. Proteins were linked to the C-terminus of TolAIII by a short flexible linker containing sites for endopeptidases. Three...