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Titolo:
Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion
Autore:
Thiede, B; Lamer, S; Mattow, J; Siejak, F; Dimmler, C; Rudel, T; Jungblut, PR;
Indirizzi:
Max Planck Inst Infekt Biol, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Berlin Germany D-10117 10117 Berlin, Germany
Titolo Testata:
RAPID COMMUNICATIONS IN MASS SPECTROMETRY
fascicolo: 6, volume: 14, anno: 2000,
pagine: 496 - 502
SICI:
0951-4198(2000)14:6<496:AOMCST>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
MASS-SPECTROMETRY; PROTEIN IDENTIFICATION; SEQUENCE DATABASES; 2-DIMENSIONAL ELECTROPHORESIS; IDENTIFYING PROTEINS; PEPTIDES; GENOME; BIOMOLECULES; IONIZATION; SPECTRA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Thiede, B Max Planck Inst Infekt Biol, Monbijoustr 2, D-10117 Berlin, Germany Max Planck Inst Infekt Biol Monbijoustr 2 Berlin Germany D-10117
Citazione:
B. Thiede et al., "Analysis of missed cleavage sites, tryptophan oxidation and N-terminal pyroglutamylation after in-gel tryptic digestion", RAP C MASS, 14(6), 2000, pp. 496-502

Abstract

Peptide mass fingerprinting is a powerful tool for the identification of proteins, Trypsin is the most widely used enzyme for this purpose. Therefore, 104 protein digests from human Jurkat T cells and Mycobacterium were analyzed considering missed cleavage sites, tryptophan oxidation and N-terminalpyroglutamylation, About 90% of the matched peptides with missed cleavage sites could be classified into three groups: (i) lysine and arginine with aneighbouring proline on the carboxy-terminal side, (ii) neighboring lysines/arginines, and (iii) lysines and arginines with an aspartic acid or glutamic acid residue on either the amino- or carboxyterminal side. The first group is already accounted for by search programs. The number of missed cleavage sites can be increased without reducing the precision of the database search by taking the other two groups into consideration. Peptides with tryptophan were observed in non, singly (+16 Da) and doubly (+32 Da) oxidized forms. The higher oxidized form was only observed with lower intensity in the presence of the lower oxidized form. Peptides with N-terminal glutamine were found always as pyroglutamate (-17 Da), and in the majority of cases inpairs with unmodified glutamine, These data can be used for the refinementof protein searches by peptide mass fingerprinting, Copyright (C) 2000 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 13:26:47