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  • 11
    Electronic Resource
    Electronic Resource
    1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI) (1977)
    Springer
    European biophysics journal 3 (1977), S. 303-315 
    Details
    ISSN: 1432-1017
    Keywords: NMR ; Proteinase inhibitor ; Protein modification ; Protein structure ; Basic pancreatic trypsin inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract In the 1H NMR spectra obtained at 360 MHz after digital resolution enhancement, the multiplet resonances of the methyl groups in the basic pancreatic trypsin inhibitor (BPTI) were resolved. With suitable double irradiation techniques the individual methyl resonances were assigned to the different types of aliphatic amino acid residues. Furthermore, from pH titration and comparison of the native protein with chemically modified BPTI, the resonance lines of Ala 16 in the active site and Ala 58 at the C-terminus were identified. Potential applications of the resolved methyl resonances as natural NMR probes for studies of the molecular conformations are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00535703
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  • 12
    Electronic Resource
    Electronic Resource
    The effect of nisin on murein synthesis (1980)
    Springer
    Archives of microbiology 127 (1980), S. 187-193 
    Details
    ISSN: 1432-072X
    Keywords: Antibiotics ; Murein (peptidoglycan) synthesis ; Nisin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Nisin inhibits murein synthesis with concomitant accumulation of undecaprenyl-pyrophospho-MurNAc(pentapeptide) (lipid intermediate I). This inhibition is caused by the formation of a complex between the antibiotic and lipid intermediate I. Undecaprenyl-pyrophospho-MurNAc(pentapeptide)-GlcNAc (lipid intermediate II) also forms a complex with nisin. However, when murein synthesis is inhibited by nisin, this latter complex is not formed since lipid intermediate II is no longer synthesized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00427192
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  • 13
    Electronic Resource
    Electronic Resource
    Semisynthesis of Arg15, Glu15, Met15, and Nle15-aprotinin involving enzymatic peptide bond resynthesis (1989)
    Springer
    The protein journal 8 (1989), S. 101-113 
    Details
    ISSN: 1573-4943
    Keywords: aprotinin ; bovine pancreatic trypsin inhibitor ; semisynthesis ; inhibitory specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The semisynthesis of homologues of aprotinin, the bovine pancreatic trypsin inhibitor, is described. The P1 lysine15 residue was replaced by two methods. The first procedure, which consisted of two enzymatic steps for the incorporation of other amino acids has previously been described. The second approach consisted of six steps of both enzymatic and chemical nature. The modified inhibitor, in which the lysine15-alanine16 peptide bond is hydrolyzed, was used as the starting material. All carboxyl groups of the modified inhibitor were esterified with methanol; the lysine15 methylester group was then selectively hydrolyzed. Afterward, lysine15 itself was split off. Arginine, glutamic acid, methionine, andl-2-aminohexanoic acid (norleucine, Nle) were incorporated using water-soluble carbodiimide combined with an acylation catalyst. The methylester group was used to prevent polymerization. The reactive-site peptide bonds were resynthesized using either chymotrypsin or trypsin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025082
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  • 14
    Electronic Resource
    Electronic Resource
    The Proteolytic Activity and Cleavage Specificity of Fibronectin-Gelatinase and Fibronectin-Lamininase (1999)
    Springer
    The protein journal 18 (1999), S. 403-411 
    Details
    ISSN: 1573-4943
    Keywords: Fibronectin ; FN-gelatinase ; FN-lamininase ; retroviral aspartic proteinases ; α2-macroglobulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human plasma fibronectin contains two latent aspartic proteinases, FN-gelatinase and FN-lamininase. Both enzymes can be generated and activated in the presence of Ca2+ from the purified cathepsin D-produced 190-kDa fibronectin fragment. We investigated the proteolytic activity and cleavage specificity of both enzymes in a range of pH from 3.5 to 9.0 using the B chain of oxidized bovine insulin and chromogenic peptides as substrates. The inhibition of the enzymes by several natural inhibitors from human plasma was also tested. The specificities of FN-gelatinase and FN-lamininase are similar to other major acidic proteinases, including pepsin, renin, cathepsin D, and HIV-proteinases. Both enzymes mainly hydrolyze three peptide bonds in the oxidized insulin B chain, namely Glu–Ala (residues 13–14), Tyr–Leu (residues 16–17), and Phe–Phe (residues 24–25). For the peptide substrates H-Pro-Thr-Glu-Phe-p-nitro-Phe-Arg-Leu-OH and H-Phe-Gly-His-p-nitro-Phe-Phe-Val-Leu-OMe that were cleaved the respective values of k cat/K M were 105.1 and 11.8 mM−1 sec−1 for cleavage by FN-gelatinase, and 123.2 and 15.5 mM−1 sec−1 for cleavage by FN-lamininase. The maximal activities of both enzymes were observed in a range between pH 5.6 and 6.3 and they became inactivated at a pH value above 8.4. Both FN-gelatinase and FN-lamininase were efficiently inhibited by α2-macroglobulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020684508212
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  • 15
    Electronic Resource
    Electronic Resource
    Enzymatic semisynthesis of aprotinin homologues mutated in P′ positions (1991)
    Springer
    The protein journal 10 (1991), S. 245-251 
    Details
    ISSN: 1573-4943
    Keywords: Aprotinin ; bovine pancreatic trypsin inhibitor ; enzymatic synthesis ; semisynthesis ; inhibitory specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The replacement of amino acids in the P′1 and P′2 position of aprotinin, the bovine pancreatic trypsin inhibitor, is described. Using the “modified” inhibitor as starting material, with the hydrolyzed reactive-site peptide bond Lys15-Ala16, the residues P′1 (Ala16) and P′2 (Arg17) were split off by the action of aminopeptidase K. Incorporation of suitable dipeptides containing a basic residue (Lys or Arg) in the C-terminal position was carried out in a “one pot” reaction involving trypsin-catalyzed coupling. In this way, the native fragment Ala16-Arg17 was reintroduced and also replaced by Gly-Arg, Ala-Lys, and Leu-Arg yielding intact inhibitor molecules. The mechanism for incorporation of dipeptides was investigated by treating the aprotinin derivative with the Arg17-Ile18 peptide bond hydrolyzed with trypsin under proteosynthetic conditions. We established that only inhibitor molecules cleaved between Lys15 and Xaa16 are intermediates leading to the desired products. The inhibitory properties of the new aprotinin homologues were tested, and the significance of the P′1 residue for the inhibition of trypsin, kallikrein, and chymotrypsin was deduced.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024788
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  • 16
    Electronic Resource
    Electronic Resource
    Chemical semisynthesis of aprotinin homologues and derivatives mutated inp′ positions (1991)
    Springer
    The protein journal 10 (1991), S. 527-533 
    Details
    ISSN: 1573-4943
    Keywords: Aprotinin ; bovine pancreatic trypsin inhibitor ; semisynthesis ; inhibitory specificity ; kallikrein inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract An extended concept for the replacement of amino acids in theP' region of aprotinin by chemical semisynthesis is presented. Either fragment condensation with dipeptides protected as tert-butyl ester or stepwise introduction of two single amino acid-tert-butyl esters into a partially esterified aprotinin derivative (with free Lys15-carboxyl group) lacking the amino acids Ala16 and Arg17 leads to aprotinin homologues and derivatives mutated in theP′ 1 andP′ 2 position. This method may complement the recently reported enzymatic synthesis by enabling access to aprotinin homologues and derivatives, which cannot be prepared enzymatically. The synthesis of [Ala17]BPTI and [seco-17/18]BPTI is described in detail.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025481
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  • 17
    Electronic Resource
    Electronic Resource
    ThepH dependence of the equilibrium constantK Hyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond in bovine pancreatic trypsin inhibitor (aprotinin) (1988)
    Springer
    The protein journal 7 (1988), S. 633-640 
    Details
    ISSN: 1573-4943
    Keywords: proteinase inhibitor ; aprotinin ; reactive-site peptide bond hydrolysis ; equilibrium constant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract ThepH dependence of the equilibrium constant KHyd for the hydrolysis of the Lys15-Ala16 reactive-site peptide bond of the bovine pancreatic trypsin inhibitor (aprotinin) was investigated over thepH range 2.3–6.5. Solutions of aprotinin, modified aprotinin with the Lys15-Ala16 peptide bond cleaved and mixtures of both species were incubated with 10 mol% porcine β-trypsin. The state of equilibrium was determined by analytical cation-exchange HPLC. The KHyd values obtained did not exactly obey the simple equation of Dobry et al. (1952), which had to be used in an extended form with two additional parameters for a satisfactory fit. ThepH-independent equilibrium constant is 0.90 and thepK values of the Lys15 carboxyl group and of the Ala16 amino group are 3.10 and 8.22, respectively. ThepK of an additional group is apparently perturbed by the peptide-bond hydrolysis. It is 4.60 in the native and 4.40 in the modified aprotinin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024879
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  • 18
    Electronic Resource
    Electronic Resource
    Expression, Purification, Characterization, and X-Ray Analysis of Selenomethionine 215 Variant of Leukocyte Collagenase (1997)
    Springer
    The protein journal 16 (1997), S. 637-650 
    Details
    ISSN: 1573-4943
    Keywords: Matrix metalloproteinases ; Met-turn ; Selenomethionine ; conformational stability ; X-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Matrix metalloproteinases belong to the superfamily of metzincins containing, besides a similar topology and a strictly conserved zinc environment, a 1,4-tight turn with a strictly conserved methionine residue at position three (the so called Met-turn [Bode et al. (1993) FEBS 331, 134–140; Stöcker et al. (1995) Protein Sci. 4, 823–840]. The distal S–CH3 moiety of this methionine residue forms the hydrophobic basement of the three His residues liganding the catalytic zinc ion. To assess the importance of this methionine, we have expressed the catalytic domain of neutrophil collagenase (rHNC, residues Met80–Gly242) in the methionine auxotrophic Escherichia coli strain B834[DE3](hsd metB), with the two methionine residues replaced by Selenomethionine. Complete replacement was confirmed by amino acid analysis and electrospray mass spectrometry. The folded and purified enzyme retained its catalytic activity, but showed modifications which are reflected in changed kinetic parameters. The Met215SeMet substitution caused a decrease in conformational stability upon urea denaturation. The X-ray crystal structure of this Selenomethionine rHNC was virtually identical to that of the wild-type catalytic domain except for a very faint local disturbance around the sulfur-seleno substitution site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026327125333
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  • 19
    Electronic Resource
    Electronic Resource
    Inhibition of Tryptase TL2 from Human T4+ Lymphocytes and Inhibition of HIV-1 Replication in H9 Cells by Recombinant Aprotinin and Bikunin Homologues (1997)
    Springer
    The protein journal 16 (1997), S. 651-660 
    Details
    ISSN: 1573-4943
    Keywords: Kunitz-type inhibitor ; aprotinin ; bikunin ; tryptase TL2 ; HIV infection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The serine esterase TL2 from human T4+ lymphocytes is a binding component to HIV-1 glycoprotein gp120 and seems to play a role in the HIV-1 infection mechanism. Recombinant variants of the Kunitz-type serine proteinase inhibitor aprotinin were investigated for their ability to inhibit tryptase TL2 and the binding of gp120 to this enzyme. Furthermore, the viral replication of HIV-1 was investigated in H9 cell cultures under the influence of recombinant aprotinin and bikunin variants. In contrast to native aprotinin, the recombinant variant [Arg15, Phe17, Glu52]aprotinin with a reactive-site sequence homologous to the V3 loop of HIV-1 gp120 showed a specific inhibition of tryptase TL2 (〉80%). However, the [Leu15, Phe17, Glu52]aprotinin variant with hydrophobic subsites was the most potent inhibitor of the binding of gp120 to tryptase TL2 (68%). Our results show that the enzyme activity of purified tryptase TL2 is inhibited not only by variants with basic amino acids, but also those with hydrophobic residues in the reactive-site region. Therefore, tryptase TL2 is not a typical trypsin-like or chymotrypsin-like protease. Investigations on inhibition of HIV-1 replication in H9 cell cultures showed that tryptase TL2 is involved in the mechanism of virus internalization into human lymphocytes. The [Leu15, Phe17, Glu52]aprotinin showed a significant retardation of syncytium formation over a period of 5 days in a 1 μM concentration. Similar investigations were performed with recombinant variants of bikunin, the light chain of human inter-α-trypsin inhibitor. Only the single-headed variant [Arg94]82bikunin inhibited slightly the syncytium formation over a period of 2 days in a 2.2 μM concentration. Wild-type bikunin and all full-length variants showed no effect, possibly due to steric hindrance by the second domain of the double-headed inhibitor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026379109403
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  • 20
    Electronic Resource
    Electronic Resource
    The Proteolytic Activity of the Recombinant Cryptic Human Fibronectin Type IV Collagenase from E. coli Expression (2000)
    Springer
    The protein journal 19 (2000), S. 685-692 
    Details
    ISSN: 1573-4943
    Keywords: Fibronectin ; type IV collagenase ; metalloprotease ; TIMP-2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human plasma fibronectin (pFN) contains a cryptic metalloprotease present in the collagen-binding domain. The enzyme could be generated and activated in the presence of Ca2+ from the purified 70-kDa pFN fragment produced by cathepsin D digestion. In this work we cloned and expressed the metalloprotease, designated FN type IV collagenase (FnColA), and a truncated variant (FnColB) in E. coli. The recombinant pFN protein fragment was isolated from inclusion bodies, and subjected to folding and autocatalytic degradation in the presence of Ca2+, and yielded an active enzyme capable of digesting gelatin, helical type II and type IV collagen, α- and β-casein, insulin b-chain, and a synthetic Mca-peptide. In contrast, isolated plasma fibronectin, type I collagen, and the DNP-peptide were no substrates. Both catalytically active recombinant pFN fragments were efficiently inhibited by EDTA, and batimastat, and, in contrast to the glycosylated enzyme isolated from plasma fibronectin, were also inhibited by TIMP-2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007104420017
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