Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal α-mannosidase B
Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal α-mannosidase B
Human lysosomal alpha-mannosidase has been purified by a simple and rapid method in sufficient quantities for the analysis of its subunit composition and partial protein sequencing. Analysis of the N-terminal residues of the 30 kDa polypeptide has enabled us to confirm the identity of the recently cloned cDNA that was tentatively identified as that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Biochem. Biophys. Res. Commun. 200, 239-245] and to locate the position of this polypeptide within the total deduced amino acid sequence. This finding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.
- Sapienza University of Rome Italy
- Roma Tre University Italy
- King's College London United Kingdom
- University of Perugia Italy
DNA, Complementary, Leukemia, Sulfates, Molecular Sequence Data, Zinc Sulfate, Zinc Compounds, alpha-Mannosidase, Enzyme Stability, Mannosidases, Tumor Cells, Cultured, Humans, Amino Acid Sequence, Lysosomes, Sequence Analysis
DNA, Complementary, Leukemia, Sulfates, Molecular Sequence Data, Zinc Sulfate, Zinc Compounds, alpha-Mannosidase, Enzyme Stability, Mannosidases, Tumor Cells, Cultured, Humans, Amino Acid Sequence, Lysosomes, Sequence Analysis
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