Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA

被引：21

作者：

Beccari, T

Appolloni, MG

Costanzi, E

Stinchi, S

Stirling, JL

DellaFazia, MA

Servillo, G

Viola, MP

Orlacchio, A

机构：

[1] UNIV LONDON KINGS COLL,DIV LIFE SCI,LONDON W8 7AH,ENGLAND

[2] UNIV PERUGIA,MONTELUCE POLICLIN,IST PATOL GEN,I-06126 PERUGIA,ITALY

来源：

BIOCHEMICAL JOURNAL | 1997年 / 327卷

关键词：

D O I：

10.1042/bj3270045

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：

Lysosomal alpha-D-mannosidase from mouse tissues was separated into its constituent isoenzymes by DEAE-cellulose chromatography. Forms corresponding to the human isoenzymes B and A were present in testis, brain, spleen and kidney, whereas in epididymis and liver only the B form was present. Murine alpha-mannosidases A and B are glycoproteins and have pH optima, thermal stabilities and molecular masses similar to those of the human isoenzymes. A full-length cDNA. (3.1 kb) containing the complete coding sequence for alpha-mannosidase was isolated from a mouse macrophage cDNA library. Comparison of the deduced amino acid sequences of human and mouse alpha-mannosidases showed that they had 75% identity and 83% similarity. Expression of this cDNA in COS cells showed that both the A and the B isoenzymes can arise from a single transcript. Northern blotting analysis showed a 10-fold range in the abundance of alpha-mannosidase mRNA in mouse tissues, with the highest levels found in epididymis, and the lowest in liver.

引用

页码：45 / 49

页数：5

共 20 条

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