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Digitale Medien

Structural analysis of protein variants by mass spectrometry: Characterization of haemoglobin providence using a grand-scale mass spectrometer (1989)

Wada, Y. ; Fujita, T. ; Hayashi, A. ; [weitere]

Chichester : Wiley-Blackwell

Biological Mass Spectrometry 18 (1989), S. 563-565

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ISSN: 0887-6134

Schlagwort(e): Chemistry ; Analytical Chemistry and Spectroscopy

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Chemie und Pharmazie

Notizen: A grand-scale mass spectrometer with high mass resolution and high transmission was employed for the analysis of haemoglobin variant. Two variants were isolated from a haemolysate by chromatography. Secondary ion mass spectrometry of complex peptide mixtures derived from these variants precisely determined the molecular weight of abnormal peptides. The molecular weight, 2857.4 and 2858.4, indicated the amino acid substitutions of asparagine and aspartic acid, respectively, for lysine at position 82 of β globin chain. The mutations had been reported in haemoglobin Providence.

Zusätzliches Material: 2 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/bms.1200180809

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Digitale Medien

Field desorption mass spectra of tryptic peptides of human hemoglobin chains (1981)

Matsuo, T. ; Matsuda, H. ; Katakuse, I. ; [weitere]

Chichester : Wiley-Blackwell

Biological Mass Spectrometry 8 (1981), S. 25-30

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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

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