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Titolo:
Structural studies on sugar chains of carbohydrate-deficient transferrin from patients with alcoholic liver disease using lectin affinity electrophoresis
Autore:
Inoue, T; Yamauchi, M; Ohkawa, K;
Indirizzi:
Jikei Univ, Sch Med, Dept Internal Med 1, Minato Ku, Tokyo 1050003, Japan Jikei Univ Tokyo Japan 1050003 al Med 1, Minato Ku, Tokyo 1050003, Japan Jikei Univ, Sch Med, Dept Biochem 1, Tokyo 1050003, Japan Jikei Univ Tokyo Japan 1050003 Med, Dept Biochem 1, Tokyo 1050003, Japan
Titolo Testata:
ELECTROPHORESIS
fascicolo: 3, volume: 20, anno: 1999,
pagine: 452 - 457
SICI:
0173-0835(199903)20:3<452:SSOSCO>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERUM TRANSFERRIN; BETA-HEXOSAMINIDASE; CONSUMPTION; MICROHETEROGENEITY; OLIGOSACCHARIDES; CHROMATOGRAPHY; CARCINOMA; PROTEINS; ETHANOL; MARKER;
Keywords:
carbohydrate-deficient transferrin; alcoholic liver disease; lectin affinity electrophoresis; sodium dodecyl sulfate-polyacrylamide gel electrophoresis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Inoue, T Jikei,Univ, Sch Med, Dept Internal Med 1, Minato Ku, 3-25-8 NishiShinbashi Jikei Univ 3-25-8 Nishi Shinbashi Tokyo Japan 1050003 Shinbashi
Citazione:
T. Inoue et al., "Structural studies on sugar chains of carbohydrate-deficient transferrin from patients with alcoholic liver disease using lectin affinity electrophoresis", ELECTROPHOR, 20(3), 1999, pp. 452-457

Abstract

It is well-known that microheterogeneity of human serum transferrin observed in alcoholics manifests as sialic acid-deficient transferrin isoforms, otherwise known as carbohydrate-deficient transferrin (CDT). A recent study demonstrated that serum CDT lacked one or both of the entire carbohydrate chains but the investigation required several troublesome procedures. The aim of the present study was to confirm the sugar chain structures of serum transferrin, and of serum CDT in particular, from patients with alcoholic liver disease (ALD) using conventional lectin affinity electrophoresis which might be useful in the clinical setting. The serum CDT obtained from ALD-patients was partially purified using an anion exchanger. Serum transferrin and the partially purified serum CDT were investigated by concanavalin A (Con A)- and Datura stramonium agglutinin (DSA)-affinity electrophoresis followed by antibody-affinity blotting and sodium dodecyl sulfate-polyacrylamidegel electrophoresis (SDS-PAGE) with Western blotting. By Con A-affinity electrophoresis, serum CDT was separated into weakly reactive and nonreactivetransferrins which showed slower electrophoretic mobilities than those from the healthy controls. Moreover, nearly all of the serum CDT was nonreactive with DSA. On SDS-PAGE, the molecular masses of serum CDT were estimated to be approximately 75 and 72 kDa, which corresponded to those of partiallyand completely deglycosylated transferrin obtained from the healthy controls (78 kDa), respectively. In conclusion, these results indicated that the sugar chain structures of serum CDT from patients with ALD show not merely a loss of terminal sialic acids, but also the absence of asparagine-N-linked oligosaccharides.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 00:35:54