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Titolo:
IDENTIFICATION OF NITRATION SITES ON SURFACTANT PROTEIN-A BY TANDEM ELECTROSPRAY MASS-SPECTROMETRY
Autore:
GREIS KD; ZHU S; MATALON S;
Indirizzi:
UNIV ALABAMA,DEPT ANESTHESIOL,619 S 19TH ST BIRMINGHAM AL 35233 UNIV ALABAMA,DEPT ANESTHESIOL BIRMINGHAM AL 35233 UNIV ALABAMA,DEPT BIOCHEM & MOL GENET BIRMINGHAM AL 35233 UNIV ALABAMA,DEPT PHYSIOL & BIOPHYS BIRMINGHAM AL 35233 UNIV ALABAMA,DEPT PEDIAT BIRMINGHAM AL 35233
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 2, volume: 335, anno: 1996,
pagine: 396 - 402
SICI:
0003-9861(1996)335:2<396:IONSOS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
PULMONARY SURFACTANT; NITRIC-OXIDE; II CELLS; PEROXYNITRITE; APOPROTEIN; SUPEROXIDE; BINDING; RESIDUES; CALCIUM; INJURY;
Keywords:
SURFACTANT APOPROTEIN; GLYCOPROTEIN; REACTIVE NITROGEN SPECIES; NITROTYROSINE; LIPID AGGREGATION; TANDEM MASS SPECTROMETRY; PEPTIDE SEQUENCING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
K.D. Greis et al., "IDENTIFICATION OF NITRATION SITES ON SURFACTANT PROTEIN-A BY TANDEM ELECTROSPRAY MASS-SPECTROMETRY", Archives of biochemistry and biophysics, 335(2), 1996, pp. 396-402

Abstract

Previous studies have shown that exposure of human surfactant proteinA (SP-A) to nitrating agents [peroxynitrite (ONOO-); tetranitromethane (TNM; pH 8)] leads to nitrotyrosine formation. However, specific sites of nitration have not been identified. Herein, human SP-A, dissolved in Hepes buffer, was incubated with two boluses each of 0.5 mM ONOO-(pH 7.4) or 0.5 mM TNM (pH 8.0) for 15 min, After 30 min, SP-A samples were reduced, alkylated, and trypsin digested. The nitrated peptidesand sites of amino acid nitration on the protein were identified by capillary high-performance liquid chromatography-coupled electrospray ionization tandem mass spectrometry (LC-ESMS/MS). The major nitrated peptide on both TNM- and ONOO--exposed SP-A was the tryptic fragment Tyr(161)-Arg(179) (YNTYAYVGLTEGPSPGDFR), located in the SP-A carbohydraterecognition domain. Sequencing of this nitrated peptide by LC-ESMS/MSdemonstrated that the nitration was equally distributed on Tyr(164) and Tyr(166). A second lesser nitrated peptide corresponding to trypticfragment Asn(217)-Arg(222) (NCLYSR) was also found on TNM- and ONOO--modified SP-A. No other nitrated amino acid was detected, Nitrated SP-A exhibited decreased ability to aggregate surfactant lipids in the presence of Ca2+. These data demonstrate that nitration of a specific tyrosine decreased an important protein function. (C) 1996 Academic Press, Inc.

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Documento generato il 27/11/20 alle ore 21:20:37