CORE-SPECIFIC LYSOSOMAL ALPHA(1-6)-MANNOSIDASE ACTIVITY DEPENDS ON ASPARTAMIDOHYDROLASE ACTIVITY

被引：15

作者：

HAEUW, JF

GRARD, T

ALONSO, C

STRECKER, G

MICHALSKI, JC

机构：

[1] UNIV SCI & TECH LILLE, CHIM BIOL LAB, F-59655 VILLENEUVE DASCQ, FRANCE

[2] UNIV SCI & TECHOL LILLE, CNRS, UNITE MIXTE RECH 11, F-59655 VILLENEUVE DASCQ, FRANCE

来源：

BIOCHEMICAL JOURNAL | 1994年 / 297卷

关键词：

D O I：

10.1042/bj2970463

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The substrate specificity of the core-specific rat liver lysosomal alpha(1-6)-mannosidase was investigated using mannosylated oligosaccharides and glycoasparagines. Hydrolysis of Man(alpha 1-6) linkage hydrolysis was demonstrated to follow the action of endoglycosidases, namely aspartyl-N-acetyl-beta-D-glucosaminidase and endo-N-acetyl-beta-D-glucosaminidase. The results are discussed with respect to the nature of the carbohydrate materials stored in the tissues and excreted in the urine from patients suffering from aspartylglucosaminuria and fucosidosis.

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页码：463 / 466

页数：4

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