Immunoaffinity purification and characterisation of p29--an estrogen receptor related protein

J Steroid Biochem Mol Biol. 1990 Nov 30;37(4):513-9. doi: 10.1016/0960-0760(90)90395-2.

Abstract

p29, a 29 kDa protein recognised by D5, a monoclonal antibody prepared against partially purified cytosolic estrogen receptor (ER), has been purified to homogeneity from ZR-75-1, a human breast cancer cell line. Ammonium sulphate fractionation followed by immunoaffinity chromatography on a three column system using Protein A-Sepharose coupled D5, produced purified p29. Silver stained SDS one-dimensional polyacrylamide gel electrophoresis (PAGE) and two-dimensional PAGE showed p29 to have been purified to homogeneity. Amino acid analysis showed no unusual characteristics. Partial N-terminal sequencing studies showed that purified p29 shared a 100% homology with the sequence of a pp89, murine cytomegaloviral protein.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Ammonium Sulfate
  • Breast Neoplasms / chemistry
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Fractional Precipitation
  • Heat-Shock Proteins*
  • Humans
  • Immunoassay
  • Molecular Sequence Data
  • Myometrium / chemistry
  • Neoplasm Proteins / isolation & purification
  • Phosphoproteins / analysis
  • Phosphoproteins / chemistry
  • Phosphoproteins / isolation & purification*
  • Receptors, Estrogen*
  • Sequence Homology, Nucleic Acid
  • Tumor Cells, Cultured

Substances

  • Amino Acids
  • Heat-Shock Proteins
  • Neoplasm Proteins
  • Phosphoproteins
  • Receptors, Estrogen
  • Ammonium Sulfate