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  • Antibiotics  (1)
  • Basic pancreatic trypsin inhibitor  (1)
  • Immunosuppression and metalloproteinases  (1)
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  • 1
    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
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 127 (1980), S. 187-193 
    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
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  • 3
    ISSN: 1432-2277
    Keywords: Immunosuppression and metalloproteinases ; Metalloproteinases and immunosuppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The concentration of the metalloproteinases type I collagenase and gelatinase was measured in isolated polymorphonuclear leukocytes (PMNLs) of renal transplant recipients treated either with cyclosporin A (CyA) and prednisolone (Pr) (n=8) or azathioprine (Aza) and Pr (n=8), and of healthy subjects (n=12). PMNLs of CyA- and Aza-treated transplant patients displayed markedly higher gelatinase content (2427±489 and 3284±357 ng/107 cells) than PMNLs of controls (528±83 ng/107 cells). There was also a higher content of type I collagenase in PMNLs (3374±292 ng/107 cells) of Aza-treated patients and significantly elevated levels in PMNLs of patients receiving CyA (3625±229 ng/107 cells) compared with healthy subjects (2878±151 ng/107 cells). In contrast, neutrophil lactoferrin content was lower in transplant patients. Thus, immunosuppressive drugs may reduce the release of leukocyte proteinases, which are known for their deleterious role in proteolytic tissue and matrix breakdown. In vitro, the effects of different immunosuppressive drugs on the release of lactoferrin, collagenase and gelatinase were investigated on FMLPNTL-stimulated PMNLs isolated from healthy subjects. CyA but not Aza or Pr caused inhibition of gelatinase, collagenase and lactoferrin release.
    Type of Medium: Electronic Resource
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