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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 4 (1990), S. 541-545 
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: 252Cf plasma-desorption mass spectrometry (PDMS) has been demonstrated to provide sequence-specific fragmentation for several oligopeptides. The nature of the fragment ions observed is generally similar to that observed using liquid secondary-ion mass spectrometry (LSIMS) and can be observed using less sample than LSIMS requires, but PDMS spectra are acquired at a lower resolution. In addition, the molecular weight of some of the oligopeptides studied exceeds that which is generally accepted as within the sequence range of LSIMS. The specific series of sequence ions that predominate in the PDMS spectra appear to be related to the amino acid compositions and sequences of the oligopeptides.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Conditions were established for analyzing as little as 5 pmol of an underivatized peptide delivered in a glycerol sample matrix as a thin film onto a gold-plated copper sample stage and then bombarded with xenon fast atoms. Calibration of the fast atom bombardment high field mass spectrometer and data system was achieved using cesium iodide/glycerol as a reference. Calibration at several accelerating potentials permitted a mass range from 393 to 5941 u. Several factors were examined that contribute to the quality of the mass spectrum: components within the glycerol such as other peptides, alkali salts, acid and reducing agents; the nature of the fast atom gas; concentration of the peptide delivered to the sample stage; and the effect of the sample stage and sample matrix on sensitivity.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Under negative ionization conditions, nominal mass calibration of the fast atom bombardment high field mass spectrometer and data system was accomplished using cesium iodide/glycerol as a reference. Mass calibration at -8 kV accelerating potential extends from m/z 387 to m/z 2170 using xenon fast atoms. Negative xenon FAB mass spectra for human angiotensin I and human gastrin I complement their positive fast atom bombardment spectra. Negative xenon fast atom bombardment spectra of underivatized peptides exhibit molecular proton-abstracted ion envelopes and structurally significant fragment ions. Peptide mixture analysis under negative xenon fast atom bombardment reveals peptide molecular ion envelopes of higher relative intensities than under positive xenon fast atom bombardment.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Sixteen peptides ranging in molecular weights from 858 to 5729 were examined under positive ionization fast atom bombardment conditions employing a high field magnet mass spectrometer and data system. The contributions of the polyisotopic elements to the molecular protonated ion envelope become important in the interpretation of the data at higher mass. For masses less than 2000 u, the most abundant ion within this envelope is the monoisotopic molecular protonated ion. Above 2000 u, the most abundant ion in the envelope is a polyisotopic molecular protonated ion. Characterization of the peptide requires identification of both the molecular protonated ion envelope and significant fragment ions. Partial spectra displaying both the molecular ion and significant fragment ions are presented for mastoparan (mol. wt = 1478), somatostatin (mol. wt = 1637), bovine parathyroid hormone (1-34) (mol. wt = 4106), and bovine insulin (mol. wt = 5729). A partial spectrum for bovine ribonuclease A (mol. wt = 13673) displayed significant fragment ions that identified the protein. The types of fragment ions included those that indicated the amino acid sequence and the location of disulfide bonds. The abundance of these ions appears to be influenced by the characteristics of the noble gas fast atom beam and the sample matrix.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 12 (1985), S. 577-585 
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ten peptides containing one, two or three disulfides were examined to determine their behavior under fast atom bombardment (FAB) mass spectrometric conditions. The mass spectra for the disulfide and the reduced disulfide forms of each peptide were compared. Several factors were examined that contribute to the fast atom bombardment mass spectra of these peptides: components of the FAB matrix such as alkali cations, acids, bases and reducing agents, the intrinsic molecular properties of the intact peptide, and the effect of reducing conditions on sensitivity. The FAB mass spectra of the disulfide-containing peptides examined in this study displayed accurate molecular weight information and fragmentation which indicated the position of the disulfide in the amino acid sequence.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new approach to the direct sequencing of oligopeptides in complex mixtures is described. Mixtures of [2H0]/[2H3]-N-acetylated and N, O-permethylated peptides are analyzed by collision activated dissociation on a triple quadrupole mass spectrometer using isobutane chemical ionization. Analysis of the collision activated dissociation spectra enables peptide sequences to be deduced. Use of electron capture negative chemical ionization for the sequence analysis of neuropeptides at the picomole level is also described.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 21 (1992), S. 176-178 
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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