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- Wade, D, et al.
(författare)
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Structural analysis of Efb, a fibrinogen binding protein of Staphylococcus aureus
- 1998
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Ingår i: Protein peptide letters. - 0929-8665 .- 1875-5305. ; 5:4, s. 199-206
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Tidskriftsartikel (refereegranskat)abstract
- Staphylococcus aureus produces and secretes a small, basic protein, designated Efb, that binds to fibrinogen and seems to be required for virulence of the organism. A 3D model of Efb was developed, and it predicts that the C-terminal half of the protein contains substantial alpha-helical content. CD analysis of Efb yielded a value of 40-41% alpha-helix. Calcium and zinc both influence the interactions between Efb and fibrinogen, and an analysis of the amino acid sequence of Efb revealed the presence of consensus sequences for the binding of both metals.
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- Bergquist, Jonas, et al.
(författare)
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Identification of catecholamines in the immune system by electrospray ionization mass spectrometry.
- 1998
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Ingår i: Rapid Communications in Mass Spectrometry. - 0951-4198 .- 1097-0231. ; 12:11, s. 683-8
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Tidskriftsartikel (refereegranskat)abstract
- The first evidence that catecholamines might be present in the immune system was provided by capillary electrophoresis combined with electrochemical detection. Here, we present the first structural characterization of the endogenous catecholamines isolated from human peripheral blood mononuclear cells. Dopamine, L-DOPA and norepinephrine were detected and were identified with electrospray ionization mass spectrometry by determination of the protonated molecular species of each catecholamine and their major fragments generated in the electrospray source with a nozzle-skimmer voltage method. This technique, in conjunction with accurate mass measurement, allowed us to identify in an unfractionated sample the content of catecholamines in extracted cells in a quantitative manner, with structure-specific methodology. The data unambiguously confirm our previous tentative findings, and also strengthen the importance of the regulatory function of catecholamines in the immune system and the existence of an autocrine loop, where lymphocytes may down-regulate their own activity.
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- Davidsson, Pia, 1962, et al.
(författare)
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Clinical mass spectrometry in neuroscience. Proteomics and peptidomics.
- 2003
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Ingår i: Cellular and molecular biology (Noisy-le-Grand, France). - 0145-5680 .- 1165-158X. ; 49:5, s. 681-8
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Forskningsöversikt (refereegranskat)abstract
- In this review we discuss the merits and drawbacks with the use of proteomic and peptidomic strategies for identification of proteins and peptides in their multidimensional interactions in complex biological processes. The progress in proteomics and peptidomics during the last years offer us new challenges to study changes in the protein and peptide synthesis. These strategies also offer new tools to follow post-translational modifications and other disturbed chemical processes that may be indicative of pathophysiological alteration(s). Furthermore these techniques can contribute to improvements in the diagnosis and therapy of neurodegenerative diseases, such as Alzheimer's disease, and psychiatric diseases, as depression and post traumatic stress disorders. We also consider different practical aspects of the applications of mass spectrometry in clinical neuroscience, illustrated by example from our laboratories. The new proteomic and peptidomic strategies will further enable the progress for clinical neuroscience research.
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- Smoluch, MT, et al.
(författare)
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Nanospray mass spectrometry for identification of peptides. Application of a novel interface
- 1999
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Ingår i: Acta biochimica Polonica. - : Polskie Towarzystwo Biochemiczne (Polish Biochemical Society). - 0001-527X .- 1734-154X. ; 46:2, s. 475-481
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Tidskriftsartikel (refereegranskat)abstract
- Electrospray ionization mass spectrometry is a powerful tool for identification of biomolecules such as peptides, proteins, oligosaccharides and neurotransmitters. Recent development of the nanospray techniques, applied at ultralow flow-rates, allowed a sensitive analysis of compounds at femto/attomolar level. Here, we present application of a novel nanospray device for the analysis and fragmentation of peptides with high sensitivity on a sector instrument. The lowest applied flow-rate of the mobile phase was maintained at 50 nl/min with a sample load of 90 fmol. Nanospray also provided a complete analysis of 500 nl of the sample for over 10 min, including sequencing of as little as 40 pmol of a substance. Such analysis provides full structural information necessary to identify the molecules.
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- Tan No, K, et al.
(författare)
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Intrathecal administration of p-hydroxymercuribenzoate or phosphoramidon/bestatin-combined induces antinociceptive effects through different opioid mechanisms
- 1998
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Ingår i: Neuropeptides. - 0143-4179 .- 1532-2785. ; 32:5, s. 411-415
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Tidskriftsartikel (refereegranskat)abstract
- The antinociceptive effect of intrathecally (i.t.) administered protease inhibitors was tested against capsaicin (800 ng) injected into the dorsal surface of a hindpaw. Both p-hydroxymercuribenzoate (2-8 nmol), a cysteine protease inhibitor, and phosphoramidon (1-4 nmol), an endopeptidase 24.11 inhibitor in the presence of bestatin (0.25 nmol) an aminopeptidase inhibitor, administered i.t. 60 min prior to the injection of capsaicin produced a dose-dependent reduction of the capsaicin-induced paw licking and biting response. p-Hydroxymercuribenzoate (4 nmol)-induced antinociception was significantly antagonized by nor-binaltorphimine, a selective kappa-opioid receptor antagonist, but not by naltrindole, a selective delta-opioid receptor antagonist. On the other hand, phosphoramidon (4 nmol) /bestatin-induced antinociception was significantly antagonized by naltrindole, but not by nor-binaltorphimine. The results indicate that the antinociceptive effect of p-hydroxymercuribenzoate may be due to the inhibition of a cysteine protease degrading endogenous dynorphins whereas phosphoramidon in the presence of bestatin blocks the degradation of enkephalins.
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