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Titolo:
Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin
Autore:
Zoellner, H; Hou, JY; Hochgrebe, T; Poljak, A; Duncan, MW; Golding, J; Henderson, T; Lynch, G;
Indirizzi:
Univ Sydney, Westmead Hosp, Dent Clin Sch, Dept Oral Pathol & Oral Med, Westmead, NSW 2145, Australia Univ Sydney Westmead NSW Australia 2145 ed, Westmead, NSW 2145, Australia Westmead Hosp, Westmead Inst Hlth Res, Westmead, NSW 2145, Australia Westmead Hosp Westmead NSW Australia 2145 , Westmead, NSW 2145, Australia Inst Immunol & Allergy Res, Westmead, NSW 2145, Australia Inst Immunol & Allergy Res Westmead NSW Australia 2145 SW 2145, Australia Univ New S Wales, Ray Williams BIomed Mass Spectrometry Facil, Sydney, NSW2052, Australia Univ New S Wales Sydney NSW Australia 2052 il, Sydney, NSW2052, Australia Univ Colorado Hlth Sci, Dept Pharmaceut Sci, Denver, CO USA Univ Colorado Hlth Sci Denver CO USA Dept Pharmaceut Sci, Denver, CO USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 284, anno: 2001,
pagine: 83 - 89
SICI:
0006-291X(20010601)284:1<83:FAMSAO>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-SERUM-ALBUMIN; GLYCATION; PROTEINS; FLUORESCENCE; MAILLARD;
Keywords:
nonenzymatic glycosylation; advanced glycation end products; serum albumin; flourometry; mass spectrometry; intramolecular movement; trypsin; CNBr; bis-ANS; acrylamide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Zoellner, H Univ Sydney, Westmead Hosp, Dent Clin Sch, Dept Oral Pathol & Oral Med, Westmead, NSW 2145, Australia Univ Sydney Westmead NSW Australia2145 , NSW 2145, Australia
Citazione:
H. Zoellner et al., "Fluorometric and mass spectrometric analysis of nonenzymatic glycosylated albumin", BIOC BIOP R, 284(1), 2001, pp. 83-89

Abstract

Albumin is the major transport protein in blood and intramolecular movement contributes to this function. Nonenzymatic glycosylation (NEG) of albuminoccurs in diabetes and, in this study, fluorometric methods were used to determine the effect of increasing levels of NEG upon intramolecular movement in human serum albumin. Low levels of NEG significantly reduced and left-shifted Trp fluorescence, reduced quenching by acrylamide and inhibited penetration of bis-ANS, while these changes became only modestly more pronounced at higher levels of NEG. Mass spectrometry of tryptic and CNBr NEG-HSA fragments identified potential glycosylation sites and demonstrated only late glycosylation of the C- and N-terminal regions of the protein. Similar changes in diabetes may contribute to altered transport function in these patients, (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 16:10:20