[Antigenic properties of heterogeneous nuclear ribonucleoprotein particles weakly binding nonhistone proteins and proteins binding single-stranded DNA (SSB proteins) from Ehrlich ascites tumor]

Ukr Biokhim Zh (1978). 1991 Sep-Oct;63(5):26-32.
[Article in Russian]

Abstract

Antigenic properties of the proteins of heterogeneous nuclear ribonucleoprotein particles, (hnRNP), weakly bound nonhistone chromatin proteins (WB(N)P) and single-strand DNA-binding proteins (SSB proteins) from chromatin and extrachromatin fraction of the Ehrlich ascites tumor cells have been comparatively studied. The chromatin and extrachromatin SSB proteins displayed similar mobility in the tube and slab SDS/PAGE, had the same ssDNA-binding capacity and similarly stimulated the replicative synthesis in permeable cells. However, the chromatin SSB proteins contained 1.4 times higher phosphate amount than the extrachromatin ones (3.1 and 2. 2. moles phosphorus per 1 mole protein, respectively). The study of four protein groups with the use of a rabbit antiserum to/against extrachromatin SSB proteins (titer 1:13000 by enzyme immunoassay) showed that the chromatin and the extrachromatin SSB proteins have similar antigenic properties. One fraction of the hnRNP proteins was also reactive with the antiserum, whereas the WB(N)P displayed no cross-reactivity. The specificity of the ferm "SSB proteins" as applied to eukaryotic cells, their affinity with hnRNP proteins and differences from the HMG proteins are discussed.

Publication types

  • Comparative Study
  • English Abstract

MeSH terms

  • Animals
  • Antigens / analysis*
  • Carcinoma, Ehrlich Tumor / immunology*
  • Chromosomal Proteins, Non-Histone / immunology*
  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / immunology*
  • Mice
  • Neoplasm Proteins / immunology*
  • Protein Binding
  • Ribonucleoproteins / immunology*

Substances

  • Antigens
  • Chromosomal Proteins, Non-Histone
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Neoplasm Proteins
  • Ribonucleoproteins