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  • 1
    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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  • 2
    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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    Paper (German National Licenses)
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