Plasma desorption mass spectrometry of haemoglobin tryptic peptides for the characterization of a Hungarian α-chain variant

S‐Aminoethylated‐αA and ‐βA globin tryptic peptides separated by reversed‐phase high‐performance liquid chromatography have been analysed by plasma desorption mass spectrometry. Almost all the expected αA and βA tryptic fragments were tentatively assigned relative to the known globin chain sequences...

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Veröffentlicht in:Biological Mass Spectrometry 1991-10, Vol.20 (10), p.579-584
Hauptverfasser: Jensen, O. Nørregaard, Roepstorff, P., Rozynov, B., Horanyi, M., Szelenyi, J., Hollan, S. R., Aseeva, E. A., Spivak, V. A.
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Sprache:eng
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Zusammenfassung:S‐Aminoethylated‐αA and ‐βA globin tryptic peptides separated by reversed‐phase high‐performance liquid chromatography have been analysed by plasma desorption mass spectrometry. Almost all the expected αA and βA tryptic fragments were tentatively assigned relative to the known globin chain sequences based on the molecular weight obtained by plasma desorption mass spectrometric analysis of the purified peptides. The application of plasma desorption mass spectrometry for structure elucidation of a haemoglobin α‐chain variant revealed the first case of Hb Hasharon in Hungary.
ISSN:1052-9306
1096-9888
DOI:10.1002/bms.1200201002