Partial sequence of the purified protein confirms the identity of cDNA coding for human lysosomal alpha-mannosidase B

Biochem J. 1995 Jan 15;305 ( Pt 2)(Pt 2):363-6. doi: 10.1042/bj3050363.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • DNA, Complementary / genetics
  • Enzyme Stability
  • Humans
  • Leukemia / enzymology
  • Lysosomes / enzymology*
  • Mannosidases / chemistry*
  • Mannosidases / drug effects
  • Mannosidases / genetics
  • Mannosidases / isolation & purification
  • Molecular Sequence Data
  • Sequence Analysis
  • Sulfates / pharmacology
  • Tumor Cells, Cultured
  • Zinc Compounds / pharmacology
  • Zinc Sulfate
  • alpha-Mannosidase

Substances

  • DNA, Complementary
  • Sulfates
  • Zinc Compounds
  • Zinc Sulfate
  • Mannosidases
  • alpha-Mannosidase

Associated data

  • GENBANK/U05572