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579 related items for PubMed ID: 129327

  • 1. Replacement of lysine by arginine, phenylalanine and tryptophan in the reactive site of the bovine trypsin-kallikrein inhibitor (Kunitz) and change of the inhibitory properties.
    Jering H, Tschesche H.
    Eur J Biochem; 1976 Jan 15; 61(2):453-63. PubMed ID: 129327
    [Abstract] [Full Text] [Related]

  • 2. Preparation and characterization of the active derivative bovine trypsin-kallikrein inhibitor (Kunitz) with the reactive site lysine-15 -- alanine-16 hydrolyzed.
    Jering H, Tschesche H.
    Eur J Biochem; 1976 Jan 15; 61(2):443-52. PubMed ID: 942916
    [Abstract] [Full Text] [Related]

  • 3. Hydrolysis-resynthesis equilibrium of the lysine-15--alanine-16 peptide bond in bovine trypsin inhibitor (Kunitz).
    Tschesche H, Kupfer S.
    Hoppe Seylers Z Physiol Chem; 1976 Jun 15; 357(6):769-76. PubMed ID: 8370
    [Abstract] [Full Text] [Related]

  • 4. Kinetics of binding of bovine trypsin-killikrein inhibitor (K unitz) in which the reactive-site peptide bond Lys-15--Ala-16 is cleaved, to alpha-chymotrypsin and beta-trypsin.
    Quast U, Engel J, Steffen E, Mair G, Tschesche H, Jering H.
    Eur J Biochem; 1975 Apr 01; 52(3):505-10. PubMed ID: 1242085
    [Abstract] [Full Text] [Related]

  • 5. Enzymatic semisynthesis of aprotinin homologues mutated in P' positions.
    Groeger C, Wenzel HR, Tschesche H.
    J Protein Chem; 1991 Apr 01; 10(2):245-51. PubMed ID: 1718310
    [Abstract] [Full Text] [Related]

  • 6. The effect of cleaving the reactive-site peptide bond Lys-15--Ala-16 on the conformation of bovine trypsin-kallikrein inhibitor (K unitz) as revealed by solvent-perturbation spectra, circular dichroism and fluorescence.
    Quast U, Engel J, Steffen E, Tschesche H, Jering H, Kupfer S.
    Eur J Biochem; 1975 Apr 01; 52(3):511-4. PubMed ID: 1242086
    [Abstract] [Full Text] [Related]

  • 7. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities.
    Scheidig AJ, Hynes TR, Pelletier LA, Wells JA, Kossiakoff AA.
    Protein Sci; 1997 Sep 01; 6(9):1806-24. PubMed ID: 9300481
    [Abstract] [Full Text] [Related]

  • 8. Thermodynamic criterion for the conformation of P1 residues of substrates and of inhibitors in complexes with serine proteinases.
    Qasim MA, Lu SM, Ding J, Bateman KS, James MN, Anderson S, Song J, Markley JL, Ganz PJ, Saunders CW, Laskowski M.
    Biochemistry; 1999 Jun 01; 38(22):7142-50. PubMed ID: 10353824
    [Abstract] [Full Text] [Related]

  • 9. Chemical-enzymatic insertion of an amino acid residue in the reactive site of soybean trypsin inhibitor (Kunitz).
    Kowalski D, Laskowski M.
    Biochemistry; 1976 Mar 23; 15(6):1309-15. PubMed ID: 1252450
    [Abstract] [Full Text] [Related]

  • 10. Replacement of lysine by arginine, phenylalanine, and tryptophan in the reactive site of the trypsin-kallikrein inhibitor (Kunitz).
    Jering H, Tschesche H.
    Angew Chem Int Ed Engl; 1974 Oct 23; 13(10):662-3. PubMed ID: 4215343
    [No Abstract] [Full Text] [Related]

  • 11. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor.
    Hochstrasser K, Albrecht G, Schönberger OL, Wachter E.
    Hoppe Seylers Z Physiol Chem; 1983 Dec 23; 364(12):1689-96. PubMed ID: 6199276
    [Abstract] [Full Text] [Related]

  • 12. Role of the S' subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, alpha-lytic protease, and cercarial protease from Schistosoma mansoni.
    Schellenberger V, Turck CW, Rutter WJ.
    Biochemistry; 1994 Apr 12; 33(14):4251-7. PubMed ID: 8155642
    [Abstract] [Full Text] [Related]

  • 13. Arginine modification in Kunitz bovine trypsin inhibitor through 1, 2-cyclohexanedione.
    Menegatti E, Ferroni R, Benassi CA, Rocchi R.
    Int J Pept Protein Res; 1977 Apr 12; 10(2):146-52. PubMed ID: 302243
    [Abstract] [Full Text] [Related]

  • 14. Changing the inhibitory specificity and function of Cucurbita maxima trypsin inhibitor-V by site-directed mutagenesis.
    Wen L, Lee I, Chen G, Huang JK, Gong Y, Krishnamoorthi R.
    Biochem Biophys Res Commun; 1995 Feb 27; 207(3):897-902. PubMed ID: 7864895
    [Abstract] [Full Text] [Related]

  • 15. Chemical-enzymatic replacement of Ile64 in the reactive site of soybeen trypsin inhibitor (Kunitz).
    Kowalski D, Laskowski M.
    Biochemistry; 1976 Mar 23; 15(6):1300-9. PubMed ID: 1252449
    [Abstract] [Full Text] [Related]

  • 16. Recombinant aprotinin homologue with new inhibitory specificity for cathepsin G.
    Brinkmann T, Schnierer S, Tschesche H.
    Eur J Biochem; 1991 Nov 15; 202(1):95-9. PubMed ID: 1718753
    [Abstract] [Full Text] [Related]

  • 17. Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies.
    Ritonja A, Turk V, Gubensek F.
    Eur J Biochem; 1983 Jun 15; 133(2):427-32. PubMed ID: 6602050
    [Abstract] [Full Text] [Related]

  • 18. Binding of native and [homoserine lactone-52]-52,53-seco-bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to porcine pancreatic beta-kallikrein-B and bovine alpha-chymotrypsin: thermodynamic study.
    Oddone R, Barra D, Amiconi G, Ascenzi P, Tarricone C, Bolognesi M, Bortolotti F, Menegatti E.
    J Mol Recognit; 1994 Mar 15; 7(1):39-46. PubMed ID: 7527234
    [Abstract] [Full Text] [Related]

  • 19. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, X. The amino-acid sequences of the trypsin-released inhibitors from horse and pig inter-alpha-trypsin inhibitors.
    Hochstrasser K, Wachter E, Albrecht GJ, Reisinger P.
    Biol Chem Hoppe Seyler; 1985 May 15; 366(5):473-8. PubMed ID: 2408637
    [Abstract] [Full Text] [Related]

  • 20. Semisynthetic aprotinin derivatives with specific alterations at the reactive-site peptide bond can be used to study structure-function relationships.
    Mehlich A, Beckmann J, Wenzel HR, Tschesche H.
    Biochim Biophys Acta; 1989 Jun 13; 996(1-2):23-9. PubMed ID: 2472174
    [Abstract] [Full Text] [Related]

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