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

Biochem Biophys Res Commun. 1989 Sep 29;163(3):1498-504. doi: 10.1016/0006-291x(89)91149-2.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Chromatography
  • Cloning, Molecular*
  • DNA / genetics*
  • Durapatite
  • Female
  • Hexosaminidases / genetics*
  • Hexosaminidases / isolation & purification
  • Hexosaminidases / metabolism
  • Humans
  • Hydroxyapatites
  • Kinetics
  • Molecular Sequence Data
  • Molecular Weight
  • Placenta / enzymology
  • Pregnancy
  • alpha-N-Acetylgalactosaminidase

Substances

  • Hydroxyapatites
  • DNA
  • Durapatite
  • Hexosaminidases
  • NAGA protein, human
  • alpha-N-Acetylgalactosaminidase

Associated data

  • GENBANK/M29276