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  • 1
    Loose Leaf
    Loose Leaf
    Augsburg : WEKA-Fachverl. für Technische Führungskräfte
    Associated volumes
    Keywords: Umweltverträgliches Produkt ; Produktentwicklung ; Recyclinggerechtes Produkt ; Produktentwicklung ; Produktentwicklung ; Umweltverträglichkeit ; Recyclinggerechtes Produkt ; Konstruktion ; Umweltverträgliches Produkt ; Produktentwicklung ; Recyclinggerechtes Produkt ; Produktentwicklung ; Produktentwicklung ; Umweltverträglichkeit ; Recyclinggerechtes Produkt ; Konstruktion
    Type of Medium: Loose Leaf
    Pages: Losebl.-Ausg.
    ISBN: 3811170775
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    Language: German
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 16 (1997), S. 651-660 
    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
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 17 (1998), S. 295-302 
    ISSN: 1573-4943
    Keywords: Xylosyltransferase ; βA4-amyloid protein precursor ; amyloid precursor-like protein 2 ; chondroitin sulfate glycosaminoglycan ; proteoglycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Acceptor affinities of UDP-D-xylose:proteoglycan core protein β-D-xylosyltransferase (XT) recognition signals in synthetic L-APP and L-APLP2 homologous peptides were determined. The Michaelis–Menten constants (K M) of the L-APP peptide TENEGSGLTNIK and the L-APLP2 peptide SENEGSGMAEQK were 20.1 and 18.9 μM, respectively. Therefore, the peptides proved to be as good acceptors for XT as the bikunin aminoterminus homologous peptide (K M = 22 μM). Due to the occurrence of L-APP and L-APLP2 transcripts in human brain tissue, XT activity was measured in human liquor cerebrospinalis. Mean values were calculated as 0.22 mU/L in males and 0.47 mU/L in females without disturbance of blood–brain barrier. In addition, in homogenized rat brain tissue a mean XT activity of 0.75 mU/L was determined. Furthermore, XT activity was investigated in 21 different human cell lines. In 7 cell lines an enzyme activity was not detected in either extracellular space or cytoplasma. Our findings indicate that XT is not ubiquitously expressed in human cell types.
    Type of Medium: Electronic Resource
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  • 4
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    Unknown
    BioMed Central
    Publication Date: 2013-09-23
    Description: Background: Propionibacteria are part of the human microbiota. Many studies have addressed the predominant colonizer of sebaceous follicles of the skin, Propionibacterium acnes, and investigated its association with the skin disorder acne vulgaris, and lately with prostate cancer. Much less is known about two other propionibacterial species frequently found on human tissue sites, Propionibacterium granulosum and Propionibacterium avidum. Here we analyzed two and three genomes of P. granulosum and P. avidum, respectively, and compared them to two genomes of P. acnes; we further highlight differences among the three cutaneous species with proteomic and microscopy approaches. Results: Electron and atomic force microscopy revealed an exopolysaccharide (EPS)-like structure surrounding P. avidum cells, that is absent in P. acnes and P. granulosum. In contrast, P. granulosum possesses pili-like appendices, which was confirmed by surface proteome analysis. The corresponding genes were identified; they are clustered with genes encoding sortases. Both, P. granulosum and P. avidum lack surface or secreted proteins for predicted host-interacting factors of P. acnes, including several CAMP factors, sialidases, dermatan-sulphate adhesins, hyaluronidase and a SH3 domain-containing lipoprotein; accordingly, only P. acnes exhibits neuraminidase and hyaluronidase activities. These functions are encoded on previously unrecognized island-like regions in the genome of P. acnes. Conclusions: Despite their omnipresence on human skin little is known about the role of cutaneous propionibacteria. All three species are associated with a variety of diseases, including postoperative and device-related abscesses and infections. We showed that the three organisms have evolved distinct features to interact with their human host. Whereas P. avidum and P. granulosum produce an EPS-like surface structure and pili-like appendices, respectively, P. acnes possesses a number of unique surface-exposed proteins with host-interacting properties. The different surface properties of the three cutaneous propionibacteria are likely to determine their colonizing ability and pathogenic potential on the skin and at non-skin sites.
    Electronic ISSN: 1471-2164
    Topics: Biology
    Published by BioMed Central
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