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Titolo:
INFLUENCE OF GLYCOSYLATION ON THE DRUG-BINDING OF HUMAN SERUM-ALBUMIN
Autore:
KOIZUMI K; IKEDA C; ITO M; SUZUKI J; KINOSHITA T; YASUKAWA K; HANAI T;
Indirizzi:
INST PASTEUR,HLTH RES FDN,INT INST TECHNOL ANAL,SAKYO KU,5F KYOTO 606JAPAN INST PASTEUR,HLTH RES FDN,INT INST TECHNOL ANAL,SAKYO KU KYOTO 606 JAPAN KITASATO UNIV,SCH PHARMACEUT SCI,MINATO KU TOKYO 108 JAPAN ASAHI CHEM IND CO LTD,DIV DIAGNOST,DIAGNOST RES & DEV DEPT,MIFU KU OHHITO SHIZUOKA 41023 JAPAN
Titolo Testata:
BMC. Biomedical chromatography
fascicolo: 4, volume: 12, anno: 1998,
pagine: 203 - 210
SICI:
0269-3879(1998)12:4<203:IOGOTD>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PERFORMANCE LIQUID-CHROMATOGRAPHY; PROTEIN-BINDING; DIABETES-MELLITUS; FRONTAL ANALYSIS; AFFINITY-CHROMATOGRAPHY; NONENZYMATIC GLYCOSYLATION; GLUCOSYLATED ALBUMIN; GLYCATED ALBUMIN; RETENTION DATA; LIVER-DISEASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
68
Recensione:
Indirizzi per estratti:
Citazione:
K. Koizumi et al., "INFLUENCE OF GLYCOSYLATION ON THE DRUG-BINDING OF HUMAN SERUM-ALBUMIN", BMC. Biomedical chromatography, 12(4), 1998, pp. 203-210

Abstract

The influence of glycosylation on the drug binding of human serum albumin (HSA) was studied using HSA containing different amounts and degrees of glycosylated HSA. The drugs used were furosemide, naproxen, procaine, phenylbutazone, salicylic acid, sulphamethoxazole, tolbutamide and warfarin. The drug-HSA parameters (lognK) were measured by the ultrafiltration method, frontal analysis and a modified Hummel-Dreyer method, The modified Hummel-Dreyer method was the simplest method with high precision and required the smallest amounts of proteins. The lognK values were well correlated with the octanol-water partition coefficients; the correlation coefficients were over 0.95. The results suggested that hydrophobic interaction is the predominant force for the drug binding. The early stage of glycosylation of HSA did not significantly affect the drug-binding capacity. Generally, the binding affinity of HSA decreased, perhaps due to a conformational change or steric hindrance (except naproxen) when further glycosylation occurred. (C) 1998 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 06:56:13