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Titolo:
Post-chromatographic detection of oligopeptides using terbium-sensitized luminescence
Autore:
Rabouan, S; Macouin, G; Prognon, P; Barthes, D;
Indirizzi:
UFR Med & Pharm, Chim Analyt Lab, F-86005 Poitiers, France UFR Med & Pharm Poitiers France F-86005 yt Lab, F-86005 Poitiers, France Fac Sci Pharmaceut & Biol Chatenay Malabry, Chim Analyt Lab, F-92290 Chatenay Malabry, France Fac Sci Pharmaceut & Biol Chatenay Malabry Chatenay Malabry France F-92290
Titolo Testata:
ANALYTICAL LETTERS
fascicolo: 13, volume: 34, anno: 2001,
pagine: 2321 - 2334
SICI:
0003-2719(2001)34:13<2321:PDOOUT>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PERFORMANCE LIQUID-CHROMATOGRAPHY; FLUORESCENCE; PEPTIDES; PROTEINS;
Keywords:
high-performance liquid chromatography; luminescence; oligopeptide; terbium; complexes;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Barthes, D UFR Med & Pharm, Chim Analyt Lab, BP 199, F-86005 Poitiers, France UFR Med & Pharm BP 199 Poitiers France F-86005 oitiers, France
Citazione:
S. Rabouan et al., "Post-chromatographic detection of oligopeptides using terbium-sensitized luminescence", ANAL LETTER, 34(13), 2001, pp. 2321-2334

Abstract

This report investigated the potential use of oligopeptide complexation with terbium III as a high-performance liquid chromatography method with time-resolved spectrofluorimetric detection for analysis of milk-derived products. The study focused on glycyl-leucyl-phenylalanine, a compound with immunostimulatory properties isolated from milk casein, and also considered tyrosine and tryptophan residues in peptides. As the water content of the mobile phase was highly restrictive for detection, acetate ions were introduced as a potentiation agent. Only post-chromatographic complexation proved feasible, because passage through a column destroyed oligopeptide-terbium chelation. Validation of glycyl-leucyl-phenylalanine, glycyl-phenylalanine, and leucyl-phenylalanine assays showed linearity in the 8 x 10(-5) to 5 x 10(-4)moll(-1) range (correlation coefficients of 0.96, 0.99 and 0.99 respectively). Results for the assay at 10(-5)mol 1(-1) showed a 7% intra-day (repeatability) coefficient of variation (CV) and a 15% inter-day (reproducibility) CV. No interferences were observed in the presence of various water-soluble vitamins present in whey. This method, when tested in the bromatology field on yoghurts with different milk origins, showed that goat wheys had phenylalanine, tyrosine, and tryptophan residues twice those of cow wheys and three times those of sheep or soja bean wheys.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:38:22