Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Affinity chromatography of branched oligosaccharides in rat liver beta-glucuronidase
Autore:
Hoja-Lukowicz, D; Litynska, A; Wojczyk, BS;
Indirizzi:
Jagiellonian Univ, Inst Zool, Dept Anim Physiol, Lab Biostruct Res, PL-30060 Krakow, Poland Jagiellonian Univ Krakow Poland PL-30060 ct Res, PL-30060 Krakow, Poland Univ Rochester, Med Ctr, Dept Pathol & Lab Med, Rochester, NY 14642 USA Univ Rochester Rochester NY USA 14642 & Lab Med, Rochester, NY 14642 USA
Titolo Testata:
JOURNAL OF CHROMATOGRAPHY B
fascicolo: 1-2, volume: 755, anno: 2001,
pagine: 173 - 183
SICI:
1387-2273(20010505)755:1-2<173:ACOBOI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTACT GOLGI PREPARATIONS; WHEAT-GERM-AGGLUTININ; STRUCTURAL ASSESSMENT; ENDOPLASMIC-RETICULUM; CARBOHYDRATE CHAINS; SUGAR CHAINS; LECTIN; GLYCOPEPTIDES; PURIFICATION; SPECIFICITY;
Keywords:
oligosaccharides; beta-glucuronidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Hoja-Lukowicz, D Jagiellonian Univ, Inst Zool, Dept Anim Physiol, Lab Biostruct Res, 6 Ingardena St, PL-30060 Krakow, Poland Jagiellonian Univ 6 Ingardena St Krakow Poland PL-30060
Citazione:
D. Hoja-Lukowicz et al., "Affinity chromatography of branched oligosaccharides in rat liver beta-glucuronidase", J CHROMAT B, 755(1-2), 2001, pp. 173-183

Abstract

Rat liver microsomal and lysosomal beta -glucuronidase-derived glycopeptides were obtained by extensive Pronase digestion followed by N-[C-14]acetylation and desialylation by neuraminidase treatment. These glycopeptides werestudied by sequential chromatography on lectin-affinity columns such as concanavalin A, lentil lectin, Phaseolus vulgaris erythroagglutinin, Ricinus communis agglutinin I, Triticum vulgaris agglutinin, Glycine max agglutininand Ulex europaeus agglutinin. Using serial lectin affinity chromatographyapproach combined with neuraminidase treatment allowed us to show the unexpected presence of complex tri- and/or tetraantennary type glycans (40.8 and 17.0% for microsomal and lysosomal enzyme, respectively). Moreover, the application of neuraminidase treatment revealed that complex biantennary type glycans, present on lysosomal beta -glucuronidase, are almost fully sialylated while the same type of glycans present on microsomal enzyme do not contain sialic acid. Furthermore, the results obtained confirmed that microsomal and lysosomal beta -glucuronidases possess high mannose and/or hybrid type glycans (19.6 and 36.6%, respectively), and complex biantennary type glycans (38.9 and 46.4%, respectively). (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 15:28:57