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  • Fibronectin  (2)
  • Gangliosides  (1)
  • Inorganic Chemistry  (1)
  • Met-turn  (1)
  • 1
    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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  • 2
    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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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    Different binding capacities of influenza A and Sendai viruses to gangliosides from human granulocytes (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 120-126 
    Details
    ISSN: 1573-4986
    Keywords: Gangliosides ; human granulocytes ; TLC overlay assay ; receptor ; influenza A virus ; Sendai virus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structures of gangliosides from human granulocytes were elucidated by fast atom bombardment mass spectrometry and by gas chromatography/mass spectrometry as their partially methylated alditol acetates. In human granulocytes besides GM3 (II3Neu5Ac-LacCer), neolacto-series gangliosides (IV3Neu5Ac-nLcOse4Cer, IV6Neu5Ac-nLcOse4Cer and VI3Neu5Ac-nLcOse6Cer) containing C24:1, and to some extent C22:0; and C16:0 fatty acid in their respective ceramide portions, were identified as major components. In this study we demonstrate that gangliosides from human granulocytes, the second most abundant cells in peripheral blood, can serve as receptors for influenza viruses A/PR/8/34 (H1N1), A/X-31 (H3N2), and a parainfluenza virus Sendai virus (HNF1, Z-strain). Viruses were found to exhibit specific adhesion to terminal Neu5Acα2-3Gal and/or Neu5Acα2-6Gal sequences as well as depending on the chain length of ganglioside carbohydrate backbones from human granulocytes, these important effector cells which represent the first line of defence in immunologically mediated reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731196
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  • 5
    Electronic Resource
    Electronic Resource
    Diphenylmethylen aus Triphenylphosphin-diphenylmethylen und aus Trimethylammonium-diphenylmethylidTeil der Dissertat. H. Tschesche, Univ. Heidelberg 1962. (1965)
    Weinheim : Wiley-Blackwell
    Berichte der deutschen chemischen Gesellschaft 98 (1965), S. 3318-3323 
    Details
    ISSN: 0009-2940
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Diphenylmethylen entstand bei der Photolyse von Triphenylphosphin-diphenylmethylen (1) und bei dem spontanen Zerfall des Trimethylammonium-diphenylmethylids (10). Es zeigte nur radikalisches Verhalten und stabilisierte sich durch Entzug von Wasserstoffatomen aus dem Lösungsmittel (bzw. dem Cyclohexen) unter Bildung von Diphenylmethan bzw. Tetraphenyläthan.  -  Mit etwa gleicher Geschwindigkeit, mit der der Zerfall des Benzhydrylids 10 erfolgte, verlief die Stevenssche Umlagerung zu [α.α-Diphenyl-äthyl]-dimethylamin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cber.19650981031
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