PARTIAL SEQUENCE OF THE PURIFIED PROTEIN CONFIRMS THE IDENTITY OF CDNA CODING FOR HUMAN LYSOSOMAL ALPHA-MANNOSIDASE-B

Human lysosomal alpha-mannosidase has been purified by a simple and ra pid method in sufficient quantities for the analysis of its subunit co mposition and partial protein sequencing. Analysis of the N-terminal r esidues of the 30 kDa polypeptide has enabled a for us to confirm the identity of the recently cloned cDNA that was tentatively identified a s that of lysosomal alpha-mannosidase [Nebes and Schmidt (1994) Bioche m. Biophys. Res. Commun. 200, 239-245] and to locate the position of t his polypeptide within the total deduced amino acid sequence. This fin ding will therefore provide a firm foundation for the characterization of alpha-mannosidosis mutations.