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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B).

In the process of molecular cloning of cDNA for proteins associated with a purified human placental sialidase fraction, we discovered one of the proteins with apparent molecular weight of 46 kDa is in reality alpha-N-acetylgalactosaminidase. The full length cDNA, pcD-HS1204, codes for 358 amino acids with the first 17 residues representing a putative signal peptide. The predicted amino acid sequence shows striking homology with human alpha-galactosidase A and yeast alpha-galactosidase. The substrate specificities as well as the behavior of the 46 kDa protein on hydroxylapatite chromatography confirmed that the 46 kDa protein is in reality alpha-N-acetylgalactosaminidase.[1]


  1. Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B). Tsuji, S., Yamauchi, T., Hiraiwa, M., Isobe, T., Okuyama, T., Sakimura, K., Takahashi, Y., Nishizawa, M., Uda, Y., Miyatake, T. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
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