A NOVEL BETA-N-ACETYLGLUCOSAMINIDASE ACTIVITY IN HOG GASTRIC-MUCOSAL MICROSOMES - PREFERENTIAL HYDROLYSIS OF TERMINAL GLCNAC-BETA-1-3 LINKAGES IN GLCNAC-BETA-1-3(GLCNAC-BETA-1-6)GAL-BETA-1-4GLCNAC, BUT GLCNAC-BETA-1-6 LINKAGES IN GLCNAC-BETA-1-3(GLCNAC-BETA-1-6)GAL

被引:6
|
作者
HELIN, J
SEPPO, A
LEPPANEN, A
PENTTILA, L
MAAHEIMO, H
NIEMELA, R
LAURI, S
RENKONEN, O
机构
[1] UNIV HELSINKI,INST BIOTECHNOL,SF-00014 HELSINKI,FINLAND
[2] UNIV HELSINKI,DEPT BIOCHEM,SF-00014 HELSINKI,FINLAND
关键词
P-N-ACETYLGLUCOSAMINIDASE; LINKAGE SPECIFICITY; OLIGO-N-ACETYLLACTOSAMINOGLYCAN; IN VITRO SYNTHESIS; HOG GASTRIC MUCOSAL MICROSOME;
D O I
10.1016/0014-5793(93)80747-I
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
Hog gastric mucosal microsomes contain beta-N-acetylglucosaminidase activity which cleaves GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc at the terminal GlcNAc beta 1-3Gal linkage faster than at the GlcNAc beta 1-6Gal bond, producing mainly GlcNAc beta 1-6Gal beta 1-4GlcNAc. In a marked contrast, GlcNAc beta 1-3(GlcNAc beta 1-6)Gal is cleaved primarily at the GlcNAc beta 1-6Gal bond, while partial hydrolysis of GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4Glc reveals similar rates of cleavage for the (1-3) and (1-6) linkages. Our data support the notion that the terminal beta 1,6-linked GlcNAc unit of GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc may interact with the reducing end GlcNAc unit intramolecularly in water solution.
引用
收藏
页码:280 / 284
页数:5
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