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'Oligopeptides' in keywords
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1996 (1)
1979 (1)
1Author    W. Tröger, C. Lippert, P. Schmidt, U. Schmidt, T. Butz, R. Hoffmann, M. ZeppezauerRequires cookie*
 Title    Hg-Coordination Studies of Cysteine Containing Oligopeptides * and the ISOLDE Collaboration 0  
 Abstract    In order to study the interaction of cysteine containing peptide chains with Hg(II) the nuclear quadrupole interaction (NQI) of 199m Hg in the Hg complex of the oligopeptide Alanine-Alanine-Cysteine-Alanine-Alanine (AACAA) was determined by time differential perturbed angular correla-tion. Different 199m Hg-NQI's for free and resin-bound AACAA were obtained. Furthermore, the 199m Hg-NQI's are influenced by the Hg:AACAA stoichiometry. 
  Reference    Z. Naturforsch. 51a, 427—430 (1996); received October 20 1995 
  Published    1996 
  Keywords    TDPAC, Nuclear quadrupole interaction, Oligopeptides, Hg-Coordination 
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 TEI-XML for    default:Reihe_A/51/ZNA-1996-51a-0427.pdf 
 Identifier    ZNA-1996-51a-0427 
 Volume    51 
2Author    Michael Przybylski, Ingo Lüderwald, Ekkehard Kraas, Wolfgang Voelter, SidneyD. NelsonRequires cookie*
 Title    Field Desorption Mass Spectra of Gastrine Peptides and Glutathione Derivatives  
 Abstract    the sequence of the C-terminal tetrapeptide of gastrine, Trp-Met-Asp-Phe-NH2, and several derivatives of glutathione, y-Glu-Cys(SR)-Gly, were characterized by field desorption mass spectrometry. The field desorption mass spectra obtained at various field ion emitter temperatures reveal abundant molecular ions and fragmentation reactions that yield partial sequence information. In the series of gluta-thione derivatives investigated, characteristic ions formed by cleavage of the y-Glu-Cys peptide bond determine the substituent at the Cys residue and can therefore be used to identify corresponding conjugation products of drug metabolites with glutathione. Introduction A variety of mass spectrometric methods for the structure analysis of oligopeptides has been devel-oped and tested in the last years [1-3]. Particularly, derivatization reactions to enhance the notoriously low volatility of peptides for mass spectral analysis have been studied extensively [4]. The most ad-vanced approach developed by Biemann et al. [5] involves multiple derivatization steps that enable the analysis of complex mixtures of di-to tetra/penta-peptides by gas chromatography-mass spectro-metry (g. c.-m.s.) using electron impact (e.i.) ioniza-tion. The value of this approach to the sequence elucidation of polypeptides containing up to 50 amino acid residues has been demonstrated [5, 6]. However, major limitations of derivatization proce-dures for the mass spectral analysis of peptides are that they require relatively large amounts of sample and present difficulties with certain polar amino acid residues. Moreover, information about chain-terminal or side chain substituents that frequently 
  Reference    Z. Naturforsch. 34b, 736—743 (1979); received December 28 1978 
  Published    1979 
  Keywords    Field Desorption Mass Spectrometry, Oligopeptides, Gastrine Peptides, Glutathione Conjugates, Molecular Ions Oligopeptides comprising 
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 TEI-XML for    default:Reihe_B/34/ZNB-1979-34b-0736.pdf 
 Identifier    ZNB-1979-34b-0736 
 Volume    34