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
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.
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页码:45 / 49
页数:5
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