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  • 1980-1984  (2)
  • Chemistry  (2)
  • Carnitine
  • Chloride transport
Datenquelle
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Erscheinungszeitraum
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Schlagwörter
  • 1
    Digitale Medien
    Digitale Medien
    Field desorption mass spectra of tryptic peptides of human hemoglobin chains (1981)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 8 (1981), S. 25-30 
    Details
    ISSN: 1052-9306
    Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Field desorption mass spectra of tryptic peptides of normal human hemoglobin α-, β-, γ-, δ-chains and abnormal β-chain of hemoglobin S were studied. Almost all mass peaks of the protonated molecular ions of tryptic peptides and many doubly charged ions were observed. The molecular weights of all tryptic peptides were estimated from the mass spectra, the heaviest mass being m/z 2955, and coincided with the values obtained from the known amino acid sequences. The different chains of hemoglobin can be distinguished by their field desorption mass spectra. The mass spectrum of abnormal β-chain of hemoglobin S (sickle-cell-anemia) showed a shift of the characteristic line due to the mutation of amino acid.
    Zusätzliches Material: 5 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/bms.1200080107
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Secondary ion mass spectra of tryptic peptides of human hemoglobin chains (1984)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 11 (1984), S. 386-391 
    Details
    ISSN: 0306-042X
    Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Secondary ion mass spectra of tryptic peprides of human globin α-, β-, γ and α-chains were studied. Almost all mass peaks of protonated molecular ions of tryptic peptides were observed and they were very stable and abundant. The present results show the possibilities for quantitative analysis of two γ-globin species: Aγ and Gγ chains, and for structural analysis of unknown abnormal hemoglobins.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/bms.1200110804
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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    Artikel (Nationallizenzen)
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