Variants of bovine pancreatic trypsin inhibitor and pharmaceutic

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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530324, 435 692, C07K 710

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active

051186683

ABSTRACT:
Peptides having essentially the sequence of bovine pancreatic trypsin inhibitor (aprotinin) wherein one or more of the amino acids at positions 15, 16, 17, 18, 34, 39 and 52 are replaced by any naturally occurring amino acid produced by recombinant DNA technology, process, expression vector and recominant host therefor and pharmaceutical use thereof. Such peptides being useful as therapeutic agents in diseases connected with the presence of excessive amounts of proteinases.

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Dayhoff et al. 1972, Atlas of Protein Sequence and Structure 5:89-99.
Tschesche et al. 1983, Adv. Exp. Med. Biol. 156A:329-337.
Tschesche et al. 1987, Biochimica et Biophysica Acta 913:97-101.
Biochemistry, vol. 16, No. 8, Apr. 19, 1977, pp. 1531-1541, Tan et al., Synthesis and characterization of a pancreatic trypsin inhibitor homologue and a model inhibitor.
The Journal of Biological Chemistry, vol. 260, No. 21, Sep. 25, 1986, pp. 11451-11455, E. Fioretti et al., Primary structure and antiproteolytic activity of a Kunitz-type inhibitor from Bovine spleen.
EMBO Journal, vol. 5, No. 12, 1986, pp. 3219-3225, B. von Wilcken-Bergmann et al., A synthetic operon containing 14 bovine pancreatic trypsin inhibitor genes is expressed in E. coli.
ADV. Exp. Med. Biol., 1983, pp. 329-337; H. Tschesche et al., Peptide/protein inhibitors of tryspin and kallikrein-primary structural requirements.
Journal of Biological Chemistry, vol. 261, No. 15, Jun. 5, 1986, pp. 7115-7118, C. Berman Marks et al., Production of native, correctly folded bovine pancreatic trypsin inhibitor by Escherichia coli.

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