Proteins S7, S10, S16 and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt

Biochim Biophys Acta. 2000 Dec 1;1494(3):213-6. doi: 10.1016/s0167-4781(00)00252-9.

Abstract

The protein components of human 40S ribosomal subunits were dissociated by centrifugation in gradients of sucrose and LiCl in the presence of 0.5 M KCl. The proteins that split off were analyzed by SDS-PAGE and 2D-PAGE. The order of dissociation of the proteins, depending on the salt concentration (from 0.8 M to 1.55 M), was established. The majority of the proteins started to split off simultaneously at a monovalent cation concentration of 0.8 M. Ten proteins were found to be more resistant; of these proteins S7, S10, S16, and S19 were retained most strongly and thereby may be considered to be core proteins.

MeSH terms

  • Electrophoresis, Gel, Two-Dimensional
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Potassium Chloride
  • Ribosomal Proteins / chemistry*
  • Ribosomes / chemistry*
  • Ultracentrifugation

Substances

  • Ribosomal Proteins
  • ribosomal protein S10
  • ribosomal protein S16
  • ribosomal protein S19
  • ribosomal protein S7
  • Potassium Chloride