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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 7 (1993), S. 20-26 
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The use of ultraviolet matrix-assisted laser desorption (MALD) to ionize peptides for analysis in a quadrupole ion trap is described. An ion source was modified to accommodate a fiber optic to transmit laser radiation from a notrogen laser (337 nm) to the tip of the sample probe containing peptide of protein samples in a matrix of 2,5-dihydroxybenzoic acid (DHB) or 3,4-dimethoxy-4-hydrexy-cinnamic acid. Detection limits are demonstrated with 10 fmol of sperm-whale-myoglobin. The dimer of sperm-whale myoglobin was also observed at m/z 34, 430. A. comparison is made of the tandem mass spectrum of (MS/MS) of human angiotensin I desorbed by MALD to that of the peptide desorbed by liquid secondary-ion mass spectrometry. Both spectra were found to contain abundant structural information.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 9 (1995), S. 1546-1551 
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The analysis of matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) mass spectra of peptides by using the cross-correlation method for database searching is illustrated. MALDI-PSD mass spectra are shown to contain sufficient fragmentation information to uniquely identify the correct amino acid sequence from large protein databases (∼160000 entries). A search employing the MALDI-PSD mass spectrum of a phosphorylated peptide that correctly identifies the amino acid sequence and the site of phosphorylation is also illustrated.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 10 (1983), S. 567-571 
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In chemical ionization mass spectrometry, the use of a noble reagent gas mixed with a proton transfer reagent gas is known to produce mass spectra which contain both protonated molecules and fragment ions. We have used a mixture of isobutane and argon to improve the mass spectra of peptides which have been derivatized to O-TMS-polyamino alcohols. The molecular weight is deduced from a prominent [M+H]+ ion; the sequence of amino acids is deduced from the usual A- and Z-series fragment ions. This technique enhances the sequence ions for lysine and glycine-containing peptides, and retains the ability to distinguish C-terminal leucine and isoleucine.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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