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Identification of some abnormal haemoglobins by fast atom bombardment mass spectrometry and fast atom bombardment tandem mass spectrometry
Author(s) -
Prome Danielle,
Prome JeanClaude,
Pratbernou Françoise,
Blouquit Yves,
Galacteros Frédéric,
Lacombe Claire,
Rosa Jean,
Robinson J. D.
Publication year - 1988
Publication title -
biomedical and environmental mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0887-6134
DOI - 10.1002/bms.1200160108
Subject(s) - fast atom bombardment , chemistry , mass spectrometry , tandem mass spectrometry , peptide , amino acid , amide , dissociation (chemistry) , ion , fragmentation (computing) , peptide sequence , protein mass spectrometry , peptide mass fingerprinting , collision induced dissociation , molecular mass , chromatography , biochemistry , enzyme , proteomics , organic chemistry , computer science , gene , operating system
The characterization of two abnormal human haemoglobins by fast atom bombardment (FAB) mapping is presented. The first variant, called ‘R’, exhibits a tryptic FAB map identical to that of normal haemoglobin. However, using Staphylococcus protease V8, a peptide containing the carboxyl end of the β‐chain exhibits a mass shift down to 300 mass units. This clearly indicates the deletion of the two last amino acids of the β‐chain. The second variant, called ‘Grenoble’, is due to two different modifications of the β‐chain. The location of the Pro → Ser exchange on peptide T 5 is achieved by the collisionally activated dissociation mass analyzed ion kinetic energy spectra of the corresponding [MH] + ion. The m / z value of that peptide indicated a supplementary acid → amide modification, which was located by amino acid sequencing using chemical methods. This work concludes with the necessity of using complementary methods for achieving rapid determinations of abnormal proteins with minute amounts.