Alterations of asparagine-linked sugar chains of N-acetyl beta-D-hexosaminidase during human renal oncogenesis: a preliminary study using serial lectin affinity chromatography

Citation
K. Yoshida et al., Alterations of asparagine-linked sugar chains of N-acetyl beta-D-hexosaminidase during human renal oncogenesis: a preliminary study using serial lectin affinity chromatography, J CHROMAT B, 723(1-2), 1999, pp. 75-80
Citations number
27
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Chemistry & Analysis
Journal title
JOURNAL OF CHROMATOGRAPHY B
ISSN journal
1387-2273 → ACNP
Volume
723
Issue
1-2
Year of publication
1999
Pages
75 - 80
Database
ISI
SICI code
1387-2273(19990219)723:1-2<75:AOASCO>2.0.ZU;2-7
Abstract
Enzymatic properties and asparagine (Asn)-linked sugar-chain structures of N-acetyl beta-o-hexosaminidase A (Hex A) were compared in human tissues bet ween normal renal cortex and renal cell carcinoma (RCC). No significant dif ferences between the two Hex A preparations were observed with respect to e nzymatic properties such as molecular mass, Michaelis-Menten value or optim al pH. With RCC preparations, relatively more Hex A passed through the conc anavalin A (Con A) column, bound weakly to Con A, or bound strongly to Con A and also to the wheat germ agglutinin (WGA) column, than with preparation s from normal renal cortex. In contrast, relatively less Hex A bound strong ly to the Con A column, but passed through the WGA column with RCC preparat ions than with those from normal renal cortex. Asn-linked sugar-chain struc tures might apparently be altered during human renal oncogenesis. (C) 1999 Elsevier Science B.V. All rights reserved.