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  • 1. Ber, B. Y.
    et al.
    Kazantsev, D. Y.
    Kalinina, E. V.
    Kovarskii, A. P.
    Kossov, V. G.
    Hallén, Anders
    KTH, Superseded Departments, Microelectronics and Information Technology, IMIT.
    Yafaev, R. R.
    Determination of nitrogen in silicon carbide by secondary ion mass spectrometry2004In: Journal of Analytical Chemistry, ISSN 1061-9348, E-ISSN 1608-3199, Vol. 59, no 3, p. 250-254Article in journal (Refereed)
    Abstract [en]

    The emission of atomic and complex nitrogen ions, which are the main impurity determining the n type conduction of silicon carbide, is investigated. It is shown that, among all the secondary ions of the CxN and SixN kind (x = 0, 1, 2, 3), the (26)(CN)(-) fragment exhibits the highest ion yield. The use of an ion peak with a specified mass as an analytical signal provides a detection limit for nitrogen in SiC at a level of 10(16) cm(-3). This result is attained in measurements at high mass resolution (M/DeltaM = 7500, interference peak (26)(C-13(2))(-)).

  • 2. Goloborod'ko, A. A.
    et al.
    Mayerhofer, Corina
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Zubarev, Alexander R.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Tarasova, I. A.
    Gorshkov, A. V.
    Zubarev, Roman A.
    Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
    Gorshkov, M. V.
    Alternative methods for verifying the results of the mass spectrometric identification of peptides in shotgun proteomics2010In: Journal of Analytical Chemistry, ISSN 1061-9348, E-ISSN 1608-3199, Vol. 65, no 14, p. 1462-1468Article in journal (Refereed)
    Abstract [en]

    Database search is the most popular approach used for the identification of peptides in contemporary shotgun proteomics; it utilizes only mass spectrometric data. In this work, we introduce three criteria for the verification of peptide identification; these are based on the analysis of data orthogonal to tandem mass spectra. The first one utilizes chromatographic retention times of peptides. The development of such approaches has been hindered by the relatively low accuracy of retention time prediction algorithms. In this work, we suggest the use of two independent models of the liquid chromatography of peptides, which increase the reliability of the results. The second criterion utilizes the mean number of missed tryptic cleavages per peptide. The third one results from the analysis of the difference between theoretical and experimentally measured peptide masses. The proposed criteria were applied to the tandem mass spectra of tryptic peptides from rat kidney tissue, which were processed by the Mascot search engine. All the criteria showed that Mascot significantly overestimated the reliability of an identification. This conclusion was supported by the PeptideProphet algorithm.

  • 3.
    Karlberg, Bo
    et al.
    Stockholm University, Faculty of Science, Department of Analytical Chemistry.
    Emons, H.
    Andersen, J. E. T.
    European analytical column no. 36 (January 2008)2009In: Journal of Analytical Chemistry, ISSN 1061-9348, E-ISSN 1608-3199, Vol. 64, no 3, p. 319-321Article in journal (Refereed)
  • 4. Samgina, T. Yu
    et al.
    Gorshkov, V. A.
    Vorontsov, Ye A.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
    Ogourtsov, S. V.
    Zubarev, R. A.
    Lebedev, A. T.
    Investigation of skin secretory peptidome of Rana lessonae frog by mass spectrometry2011In: Journal of Analytical Chemistry, ISSN 1061-9348, E-ISSN 1608-3199, Vol. 66, no 13, p. 1298-1306Article in journal (Refereed)
    Abstract [en]

    Amphibian skin secretion represents a cerain scientific interest as a source of biologically active natural peptides. In the present research skin peptidome of wide-spread European frog Rana lessonae (Camerano, 1882) was studied for the first time ever. Peptide sequencing was accomplished with Fourier transform ion cyclotron resonance mass spectrometer in collision-induced and electron capture dissociation modes. A portion of amphibian peptides contains intramolecular C-terminal disulfide cycle which obstructs mass spectrometric sequencing. Two methods were utilized to overcome this difficulty: reduction with dithiotreithol followed by thiol group alkylation and oxidation into sulfonic acid groups with performic acid. Integrated approach employed in the present study allowed the identification of 49 peptides (of 6 to 37 amino acid residues), including 19 novel species.

  • 5. Samgina, T. Yu.
    et al.
    Gorshkov, V. A.
    Vorontsov, Ye. A.
    Artemenko, Konstantin A.
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry, Analytical Chemistry.
    Ogourtsov, S. V.
    Zubarev, R. A.
    Lebedev, A. T.
    Mass spectral study of the skin peptide of brown frog Rana temporaria from Zvenigorod population2011In: Journal of Analytical Chemistry, ISSN 1061-9348, E-ISSN 1608-3199, Vol. 66, no 14, p. 1353-1360Article in journal (Refereed)
    Abstract [en]

    Skin secretions of amphibian are an interesting source of biologically active peptides. The present study provides the profile of the skin secretions of the brown frog Rana temporaria from Zvenigorod population (Russia). Sequencing of the skin secretion components has been carried out on an ion cyclotron resonance instrument with electrospray ionization and two methods of fragmentation activation, collisional activation and electron capture. For sequencing of the peptides containing intermolecular C-terminal disulfide cycle two methods of disulfide bond opening have been used: reduction with subsequent alkylation of the free thiol groups and oxidation with performic acid with the formation of sulfo-acid groups. The peptide profile of Rana temporaria studied by a complex mass spectral method has been compared with the data for the frogs of other European populations of this species. For the first time we have revealed ornithokinin-antagonist of the ornithokinin receptor-in skin secretions of amphibians.

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