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Titolo:
Determination of phosphorylation levels of tyrosine hydroxylase by electrospray mass spectrometry
Autore:
Graham, ME; Dickson, PW; Dunkley, PR; von Nagy-Felsobuki, EI;
Indirizzi:
Univ Newcastle, Fac Sci & Math, Sch Biol & Chem Sci, Newcastle, NSW 2308, Australia Univ Newcastle Newcastle NSW Australia 2308 ewcastle, NSW 2308, Australia Univ Newcastle, Fac Med & Hlth Sci, Discipline Med Biochem, Newcastle, NSW2308, Australia Univ Newcastle Newcastle NSW Australia 2308 Newcastle, NSW2308, Australia
Titolo Testata:
ANALYTICAL BIOCHEMISTRY
fascicolo: 1, volume: 281, anno: 2000,
pagine: 98 - 104
SICI:
0003-2697(20000515)281:1<98:DOPLOT>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; MULTIPROTEIN KINASE; PEPTIDE-BONDS; CLEAVAGE; CALMODULIN; ACTIVATION; ACID; 3-MONOOXYGENASE; SUBSTRATE; SERINE-31;
Keywords:
tyrosine hydroxylase; phosphorylation; electrospray mass spectrometry; aspartic acid cleavage;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: von Nagy-Felsobuki, EI Univ Newcastle, Fac Sci & Math, Sch Biol & Chem Sci, Newcastle, NSW 2308, Australia Univ Newcastle Newcastle NSW Australia 2308 tralia
Citazione:
M.E. Graham et al., "Determination of phosphorylation levels of tyrosine hydroxylase by electrospray mass spectrometry", ANALYT BIOC, 281(1), 2000, pp. 98-104

Abstract

A novel approach has been developed to quantify the extent of phosphorylation of tyrosine hydroxylase (TH). The strategy consists of a chemical cleavage and characterization of the products using electrospray mass spectrometry (ESMS). The chemical cleavage involves selective hydrolysis of the aspartyl-peptide bond. Of the peptides formed, an 8-kDa NH2-terminus fragment isfound to accurately duplicate the phosphorylation of TH using standard mixtures of TH-P/TH. The calibration yields a straight line With an R-2 Of 0.996, Which is valid within the 10-90% range. The ESMS protocol has been usedto determine the extent of phosphorylation of TH in the presence of CaM-PKII. The experimental conditions were designed to produce low levels of phosphorylation. Nevertheless, the ESMS analysis yielded single, double, and nonphosphorylation forms of TH. With respect to in vivo measurements, this ESMS protocol may be a generic procedure for determining the extent of phosphorylation of proteins. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:26:12