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Titolo:
Multiple separations facilitate identification of protein variants by massspectrometry
Autore:
Zhang, ZL; Smith, DL; Smith, JB;
Indirizzi:
Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA Univ Nebraska Lincoln NE USA 68588 aska, Dept Chem, Lincoln, NE 68588 USA
Titolo Testata:
EUROPEAN JOURNAL OF MASS SPECTROMETRY
fascicolo: 2, volume: 7, anno: 2001,
pagine: 171 - 179
SICI:
1469-0667(2001)7:2<171:MSFIOP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
AGE-RELATED-CHANGES; HUMAN LENS; CRYSTALLINS; PEPTIDES; ELECTROPHORESIS; SEQUENCE; DATABASE;
Keywords:
chromatography; gel electrophoresis; HPLC/electrospray ionization mass spectrometry; lens beta-crystallins; tandem mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Smith, JB Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA Univ Nebraska Lincoln NE USA 68588 Chem, Lincoln, NE 68588 USA
Citazione:
Z.L. Zhang et al., "Multiple separations facilitate identification of protein variants by massspectrometry", EUR J MASS, 7(2), 2001, pp. 171-179

Abstract

Identification of variant proteins from complex biological samples promises to contribute much to our understanding of the etiology of pathological states. Characterization of variants, due either to genetic mutations in protein sequences or to post-translational modifications, is considerably moredifficult than the simple protein identifications typical of most current proteomic investigations. Identification of a few peptides by database retrieval is not adequate when the goal is to have a complete understanding of the modifications of the protein. Although one advantage of mass spectrometry is its ability to obtain specific responses to several components, the complexity of biological samples is often overwhelming, resulting in spectralacking useful information. For complex mixtures, isolation procedures before mass spectrometric analysis may need to include a variety of chromatographic and electrophoretic separation techniques. In this report, we illustrate how several preparative steps were essential for obtaining information about modified human lens beta -crystallins. The preparative techniques prior to mass spectrometry included size-exclusion chromatography, reversed-phase chromatography, two-dimensional gel electrophoresis, in situ digestion of the proteins and peptide trapping and washing before a final reversed-phase high-performance liquid chromatographic separation on-line to the mass spectrometer. This approach for isolation and analysis, when customized forother proteins, should find application in many studies where protein variants of complex mixtures are to be identified.

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Documento generato il 02/04/20 alle ore 12:42:16