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Titolo:
Improved accuracy in the matrix-assisted laser desorption/ionization-mass spectrometry determination of the molecular mass of cyanogen bromide fragments of proteins by post-cleavage reaction with tris(hydroxymethyl)aminomethane
Autore:
Compagnini, A; Cunsolo, V; Foti, S; Saletti, R;
Indirizzi:
Univ Catania, Dipartimento Sci Chim, I-95125 Catania, Italy Univ Catania Catania Italy I-95125 ento Sci Chim, I-95125 Catania, Italy
Titolo Testata:
PROTEOMICS
fascicolo: 8, volume: 1, anno: 2001,
pagine: 967 - 974
SICI:
1615-9853(200108)1:8<967:IAITML>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTROSPRAY IONIZATION; PRINCIPLES; PEPTIDE;
Keywords:
matrix-assisted laser desorption/ionization-mass spectrometry; cyanogen bromide; cleavage; tris(hydroxymethyl)aminomethane; cytochrome c; lysozyme; human serum albumin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
12
Recensione:
Indirizzi per estratti:
Indirizzo: Foti, S Univ Catania, Dipartimento Sci Chim, Viale A Doria 6, I-95125 Catania, Italy Univ Catania Viale A Doria 6 Catania Italy I-95125 Catania, Italy
Citazione:
A. Compagnini et al., "Improved accuracy in the matrix-assisted laser desorption/ionization-mass spectrometry determination of the molecular mass of cyanogen bromide fragments of proteins by post-cleavage reaction with tris(hydroxymethyl)aminomethane", PROTEOMICS, 1(8), 2001, pp. 967-974

Abstract

In order to improve the accuracy in the matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) determination of the molecular mass of cyanogen bromide (CNBr) fragments of proteins, the post-cleavage reaction of these fragments with tris(hydroxymethyl)aminomethane (Tris) was tested. Mixtures of homoserine and homoserine lactone peptide fragments originating from CNBr cleavage of cytochrome c, lysozyme and human serum albumin were used as model compounds. Reaction of these fragments with Tris converts quantitatively the homoserine lactone ending peptides into the correspondingamides, leaving unmodified the homoserine ending forms. Thus, pairs of fragments which differ by 103 Da are formed. In contrast to the unmodified CNBr mixtures of peptides, which, due to the overlap of the signals of the free homoserine and homoserine lactone forms, produce unresolved peaks in the high mass region of the MALDI spectra, these pairs of fragments give resolved doublets of peaks up to a mass of 20 000 Da. This permits accurate determination of the molecular mass of the fragments. Using this procedure, differences less than 5 Da with respect to the calculated values were obtained for the fragments examined.

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Documento generato il 31/03/20 alle ore 10:05:36