title: Proteins S7, S10, S16 and S19 of the human 40S ribosomal subunit are most resistant to dissociation by salt.
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.
authors: Novosibirsk Institute of Bioorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, Lavrentiev pr. 8, Novosibirsk 630090, Russia.
authors: A A
authors: AA
authors: Malygin
authors: D D
authors: DD
authors: Shaulo
authors: G G
authors: GG
authors: Karpova
mesh_terms: D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D011189:Potassium Chloride; D012269:Ribosomal Proteins / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry*; D014461:Ultracentrifugation
chemical_list: D012269:Ribosomal Proteins; C029537:ribosomal protein S10; C023509:ribosomal protein S16; C040343:ribosomal protein S19; C037442:ribosomal protein S7; D011189:Potassium Chloride