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