Preparation and characterization of the active derivative bovine trypsin-kallikrein inhibitor (Kunitz) with the reactive site lysine-15 -- alanine-16 hydrolyzed.

No abstract is available for this paper.

• Publication year

  1976

• Venue

  European Journal of Biochemistry

• Publication date

  Unknown publication date

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1111/J.1432-1033.1976.TB10038.XPMID 942916
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Kinetics of Binding of Bovine Trypsin‐Kallikrein Inhibitor (Kunitz) in which the Reactive‐Site Peptide Bond Lys‐15‐Ala‐16 is Cleaved, to α‐Chymotrypsin and β‐Trypsin

  1975cited by this paper
• 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.

  1975cited by this paper
• 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.

  1975cited by this paper
• Proteinase catalyzed resynthesis of the peptide bond Lys 15--Ala 16 in the derivative of trypsin-kallikrein inhibitor (Kunitz) with this peptide bond hydrolyzed.

  1974cited by this paper
• Synthesis of the active derivative of bovine trypsin-kallikrein inhibitor (Kunitz) with open peptide bond in the reactive site.

  1974cited by this paper
• Darstellung des aktiven Derivates von Rinder-Trypsin-Kallikrein-Inhibitor (Kunitz) mit im reaktiven Zentrum geöffneter Peptidbindung†

  1974cited by this paper
• Biochemistry of natural proteinase inhibitors.

  1974cited by this paper
• Proteinase-katalysierte Resynthese der Peptidbindung Lys 15—Ala 16 im Derivat des Trypsin-Kallikrein-Inhibitors (Kunitz) mit geöffneter Peptidbindung†

  1974cited by this paper
• Inaktivierung des Trypsin‐Kallikrein‐Inhibitors (Kunitz) durch Abspaltung des Dipeptids Ala 16—Arg 17 im reaktiven Zentrum

  1974cited by this paper
• Biochemie natürlicher Proteinase‐Inhibitoren

  1974cited by this paper
• Reactive Site Cleavage, Thermodynamic Control Resynthesis, and Properties of Chemically Derivatized Trypsin-Kallikrein-Inhibitors

  1974cited by this paper
• Evolution of Specificity of Protein Proteinase Inhibitors

  1974cited by this paper
• Inactivation of the trypsin-kallikrein inhibitor (Kunitz) by cleavage of the dipeptide Ala 16--Arg 17 in the reactive site.

  1974cited by this paper
• Submicro-determination of amino acids by a single-column analysis in a 4-hour run using automated buffer gradient mixing.

  1973cited by this paper
• Ethanol inhibits Intestinal Calcium Transport in Rats

  1973cited by this paper
• Thermodynamics and kinetics of the reactive site peptide-bond hydrolysis in bovine pancreatic secretory trypsin inhibitor (Kazal).

  1973cited by this paper
• Peptide-bond hydrolysis equilibria in the antitrypsin site of lima bean protease inhibitor.

  1973cited by this paper
• Aminopeptidase K from Tritirachium album Limber. I. Isolation and some properties.

  1973cited by this paper
• Detailed mechanism of interaction of bovine -trypsin with soybean trypsin inhibitor (Kunitz). I. Stopped flow measurements.

  1973cited by this paper
• Protease inhibitors as snake venom toxins.

  1973cited by this paper
• Broad-specificity protease-isoinhibitors for trypsin, chymotrypsin, plasmin and kallikrein from snails (Helix pomatia). Isolation, inhibition characteristics and amino-acid composition.

  1972cited by this paper
• Broad‐Specificity Protease‐Isoinhibitors for Trypsin, Chymotrypsin, Plasmin and Kallikrein from Snails (Helix pornatia)

  1972cited by this paper
• Antitrypsin site of lima bean protease inhibitor.

  1972cited by this paper
• [New polyvalent protease inhibitors for trypsin, chymotrypsin, plasmin and kallikreins from snails (Helix pomatia)].

  1972cited by this paper
• Primary structure of trypsin inhibitor from cow colostrum (component B2)

  1971cited by this paper
• Mass Spectral Determination of Peptide Bond Hydrolysis Equilibria in Protein Proteinase-Inhibitors

  1971cited by this paper
• 11 Protein Proteinase Inhibitors-Molecular Aspects

  1971cited by this paper
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

  1970cited by this paper
• The basic trypsin inhibitor of bovine pancreas

  1970cited by this paper
• Formation from trypsin and modified soybean trypsin inhibitor of a complex which upon kinetic control dissociation yields trypsin and virgin inhibitor.

  1970cited by this paper
• [66b] Bovine trypsin-kallikrein inhibitor (kunits inhibitor, basic pancreatic trypsin inhibitor, polyvalent inhibitor from bovine organs)

  1970cited by this paper
• Identifizierung von Lysin- und Argininresten als Hemmzentren von Proteaseinhibitoren mit Hilfe von Maleinsäureanhydrid und Butandion-(2.3)

  1969cited by this paper
• Peptide-bod hydrolysis equilibria in native proteins. Conversion of virgin into modified soybean trypsin inhibitor.

  1969cited by this paper
• [Identification of lysine and arginine residues as inhibitory centers of protease inhibitors by means of maleic anhydride and butane-(2.3)-dione].

  1969cited by this paper
• On proteins. CXIV. Sequence of residues 18-20 in pancreatic trypsin inhibitor

  1968cited by this paper
• Limited proteolysis of the bovine pancreatic secretory trypsin inhibitor at acid pH.

  1968cited by this paper
• The basic typsin inhibitor of bovine pancreas. IX. Location of the reactive site in the carboxamidomethyl derivative.

  1968cited by this paper
• Preparation of leucine aminopeptidase free of endopeptidase activity.

  1968cited by this paper
• The basic trypsin inhibitor of bovine pancreas. 8. Changes in activity following substitution of reduced half-cystin res4ues 14 and 38 with sulfhydryl reagents.

  1968cited by this paper
• Resynthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor.

  1967cited by this paper
• The basic trypsin inhibitor of bovine pancreas. VII. Reduction with borohydride of disulfide bond linking half-cystine residues 14 and 38.

  1967cited by this paper
• Über Trypsininhibitoren, II. Zur Charakterisierung des spezifischen Trypsininhibitors aus Schweinepankreas

  1967cited by this paper
• [On modification of the specific trypsin inhibitor from porcine pancreas during inhibition by trypsin].

  1967cited by this paper
• The disulfide linkages in kallikrein inactivator of bovine lung.

  1966cited by this paper
• [ON THE IDENTITY OF KALLIKREIN INACTIVATOR FROM CATTLE LUNG AND CATTLE PAROTID GLAND].

  1965cited by this paper
• THE BASIC TRYPSIN INHIBITOR OF BOVINE PANCREAS. IV. THE LINEAR SEQUENCE OF THE 58 AMINO ACIDS.

  1965cited by this paper
• The basic trypsin inhibitor of bovine pancreas. V. The disulfide linkages.

  1965cited by this paper
• Notizen: Zur Identität des Kallikrein-Inaktivators aus Rinderlunge und Rinderparotis

  1965cited by this paper
• The basic trypsin inhibitor of bovine pancreas. III. A progress report on the tryptic peptides

  1964cited by this paper
• DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *

  1964cited by this paper
• [PROPERTIES AND ANALYTICAL USES OF AMINOPEPTIDASE FROM KIDNEY PARTICLES].

  1964cited by this paper
• [PRIMARY STRUCTURE OF A PANCREATIC INHIBITOR OF TRYPSIN (INHIBITOR OF KUNITZ AND NORTHROP)].

  1964cited by this paper
• The kinetics of carboxypeptidase B activity.

  1962cited by this paper
• Methoden der enzymatischen Analyse

  1962cited by this paper
• Tissue sulfhydryl groups.

  1959cited by this paper
• Automatic recording apparatus for use in the chromatography of amino acids.

  1958cited by this paper
• The oxidation of ribonuclease with performic acid.

  1956cited by this paper
• ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUND

  1936cited by this paper

• BPTI backbone variants and implications for inhibitory activity.

  2009cites this paper
• Structure of a serine protease poised to resynthesize a peptide bond

  2009cites this paper
• Functional and structural roles of the Cys14-Cys38 disulfide of bovine pancreatic trypsin inhibitor.

  2008cites this paper
• The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein.

  2003cites this paper
• Concentrations of Protease Inhibitors That Can Prevent the Initiation of Motility of Demembranated Spermatozoa *

  2002cites this paper
• 8 – Reversible Inhibitors of Serine Proteinases: Naturally Occurring Miniproteins, Semisynthetic Variants, Recombinant Homologs, and Synthetic Peptides

  1995cites this paper
• Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa derived from the Mexican leech Haementeria officinalis.

  1994cites this paper
• Interaction of Streptomyces subtilisin inhibitor (SSI) with Streptomyces griseus metallo-endopeptidase II (SGMP II).

  1993cites this paper
• Probing the determinants of disulfide stability in native pancreatic trypsin inhibitor.

  1993cites this paper
• Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: functional and structural investigation.

  1992cites this paper
• Genetic dissection of pancreatic trypsin inhibitor.

  1992cites this paper
• The hydrolysis and resynthesis of a single reactive site peptide bond in recombinant antistasin by coagulation factor Xa.

  1992cites this paper
• Enzymatic semisynthesis of aprotinin homologues mutated in P′ positions

  1991cites this paper
• Enzymatic fragment substitution as a tool in protein design.

  1991cites this paper
• Recombinant aprotinin homologue with new inhibitory specificity for cathepsin G.

  1991cites this paper
• Chemical semisynthesis of aprotinin homologues and derivatives mutated inp′ positions

  1991cites this paper
• Design of an aprotinin variant with inhibitory activity against chymotrypsin and cathepsin G by recombinant DNA technology.

  1990cites this paper
• Semisynthesis of Arg15, Glu15, Met15, and Nle15-aprotinin involving enzymatic peptide bond resynthesis

  1989cites this paper
• Semisynthetic arginine-15-aprotinin, an improved inhibitor for human plasma kallikrein.

  1989cites this paper
• Reflections on chemical modification of proteinases and their protein inhibitors.

  1988cites this paper
• Aprotinin derivatives with chromophoric leaving groups can be used as highly selective active-site titrants for serine proteinases and permit the determination of kinetic constants of enzyme-inhibitor complexes.

  1988cites this paper
• ThepH dependence of the equilibrium constantKHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin)

  1988cites this paper
• Enzymatic resynthesis of the "reactive site" bond in the modified aprotinin derivatives [seco-15/16]aprotinin and [Di-seco-15/16,39/40]aprotinin.

  1988cites this paper
• Preparation of chemically 'mutated' aprotinin homologues by semisynthesis. P1 substitutions change inhibitory specificity.

  1988cites this paper
• Characterization and sequence determination of six aprotinin homologues from bovine lungs.

  1988cites this paper
• Kinetics of inhibition of human plasma kallikrein by a site-specific modified inhibitor Arg15-aprotinin: evaluation using a microplate system and comparison with other proteases.

  1987cites this paper
• Protein engineering by chemical means?

  1987cites this paper
• Semisynthetic engineering of proteinase inhibitor homologues.

  1987cites this paper
• Effects of protease inhibitors and substrates on motility of mammalian spermatozoa

  1986cites this paper
• Dissecting the roles of individual interactions in protein stability: Lessons from a circularized protein

  1985cites this paper
• The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.

  1984cites this paper
• Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs.

  1983cites this paper
• Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor.

  1983cites this paper
• DYNAMIC ASPECTS OF PROTEIN CONFORMATION STUDIED BY NUCLEAR MAGNETIC RESONANCE TECHNIQUES: EVIDENCE FOR HYDROPHOBIC STABILITY DOMAINS IN GLOBULAR PROTEINS

  1981cites this paper
• Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino-acid residues.

  1981cites this paper
• „Chemische Mutation” durch Aminosäureaustausch im reaktiven Zentrum eines Proteinase-Inhibitors und Ånderung seiner Hemmspezifität†‡

  1981cites this paper
• Structural characterization by nuclear magnetic resonance of a reactive-site 13carbon-labelled basic pancreatic trypsin inhibitor with the peptide bond Arg-39--Ala-40 cleaved and Arg-39 removed.

  1979cites this paper
• The influence of localized chemical modifications of the basic pancreatic trypsin inhibitor on static and dynamic aspects of the molecular conformation in solution.

  1979cites this paper
• Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor.

  1979cites this paper
• Individual assignments of the methyl resonances in the 1H nuclear magnetic resonance spectrum of the basic pancreatic trypsin inhibitor.

  1978cites this paper
• NMR Studies of the Molecular Dynamics of Peptides and Proteins

  1978cites this paper
• Kinetics of the interaction of alpha-chymotrypsin with trypsin kallikrein inhibitor (Kunitz) in which the reactive-site peptide bond Lys-15--Ala-16 is split.

  1978cites this paper
• Stopped-flow kinetics of the resynthesis of the reactive site peptile bond in kallikrein inhibitor (Kunitz) by beta-trypsin.

  1978cites this paper
• Dynamic model of globular protein conformations based on NMR studies in solution

  1978cites this paper
• EVOLUTION OF AVIAN OVOMUCOIDS

  1978cites this paper
• The primary structure of the human pancreatic secretory trypsin inhibitor. Amino acid sequence of the reduced S-aminoethylated protein.

  1977cites this paper
• 1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI)

  1977influential citation
• Anhydrotrypsin: new features in ligand interactions revealed by affinity chromatography and thionine replacement.

  1977cites this paper
• 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.

  1976cites this paper