| Literature DB >> 9355733 |
T Beccari1, M G Appolloni, E Costanzi, S Stinchi, J L Stirling, M A Della Fazia, G Servillo, M P Viola, A Orlacchio.
Abstract
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.Entities:
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Year: 1997 PMID: 9355733 PMCID: PMC1218761 DOI: 10.1042/bj3270045
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857