Isolation and amino terminal sequencing of a novel melanoma-associated antigen

Arch Biochem Biophys. 1985 Nov 1;242(2):540-8. doi: 10.1016/0003-9861(85)90241-3.


The biochemical characteristics are described for a melanoma-associated glycoprotein antigen, whose expression depends on stage of tumor progression and melanocytic differentiation. This antigen, identified using a monoclonal antibody which specifically stains melanoma cells in immunoperoxidase assay of fixed tissue sections, is synthesized as a 30,000-Da precursor and then processed to a 30,000- to 60,000-Da sialylated glycoprotein. Two-dimensional gel electrophoresis of the antigen resolved more than 20 forms, heterogeneous in both charge and molecular weight. The kinetics of post-translational processing, the sensitivity of processing to tunicamycin, and the molecular weight of the oligosaccharide chains indicate that the oligosaccharides are N-linked. Amino acid sequencing of the antigen purified by immunoaffinity chromatography and by high-pressure liquid chromatography or polyacrylamide gel electrophoresis allowed the assignment of the first 20 acids.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Neoplasm
  • Cell Line
  • Humans
  • Iodine Radioisotopes
  • Melanoma / immunology*
  • Melanoma-Specific Antigens
  • Molecular Weight
  • Neoplasm Proteins / isolation & purification*
  • Radioimmunoassay


  • Antigens, Neoplasm
  • Iodine Radioisotopes
  • Melanoma-Specific Antigens
  • Neoplasm Proteins