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  • Wiley-Blackwell  (2)
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  • 1
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: It has been discovered that 1,2,3-benzenetricarboxylic acid and some 5-substituted derivatives are specific and competitive inhibitors of the mitochondrial tricarboxylate carrier. In order to characterize these acids a study was carried out using electron ionization (EI), chemical ionization (CI) and fast atom bombardment (FAB) mass spectrometry on the free acids, the potassium salt of 1,2,3-benzenetricarboxylic acid and the corresponding methyl esters.Unimolecular decomposition processes were also studied using B/E linked scan experiments in order to correlate peaks present in the FAB mass spectra of the above compounds. The FAB ionization method, as expected, was the most suitable for analysing the very polar and thermolabile acids and the only method which could be used for the analysis of the potassium salt. EI and CI turned out to be appropriate methods for analysing the less polar and thermostable trimethyl esters.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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  • 2
    ISSN: 1076-5174
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The carbohydrate moiety of human α-fetoprotein, an RMM 67000 glycoprotein produced in a hepatoma cell line (Hep G2), was investigated by the combined use of high-resolution chromatographic techniques and mass spectrometry. Fast atom bombardment mass spectrometric (FABMS) and reversed-phase high-performance liquid chromatographic analysis of α-fetoprotein obtained from a large-scale cell culture following tryptic and peptide N-glycanase F hydrolysis demonstrated that the protein contains a single glycosylation site at level of asparagine 232. Further, electrospray mass spectrometric measurement of the intact protein molecular mass showed that two main glycoforms are present. The complete definition of the structural heterogeneity of the oligosaccharide moiety was achieved by high-performance anion-exchange chromatography with pulsed amperometric detection together with carbohydrate mapping by FABMS of the released oligosaccharides demonstrating (i) that the glycosylation produced by cell culture is of the biantennary complex type typical of human hepatoma α-fetoprotein and (ii) the presence of two main structures in a ratio of about 2:1 differing in the presence of a fucose residue in the N-acetylglucosamine in the non reducing portion of the molecule.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
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