Solution of ribosomal proteins under mild conditions.
Ribosomal proteins from two eucaryotic species, prepared by either the guanidine . HCl or LiCl . urea method and subsequently dissolved in 8 M urea were found to be largely retained in solution after removal of the urea by dialysis against a solution of low ionic strength (0.05 M Tris . HCl, pH 7.6, 0.025 M KCl, 0.005 M magnesium acetate) and centrifugation at 100,000 times g. The protein composition of this preparation was virtually identical to that of the original urea-containing solution as determined by two-dimensional polyacrylamide gel electrophoresis. Thus, there exists a very simple method for obtaining the bulk of the ribosomal proteins in solution under conditions where ribosomes themselves are stable.
D000818:Animals; D001798:Blood Proteins / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006146:Guanidines; D008094:Lithium; D008722:Methods; D009994:Osmolar Concentration; D010063:Ovum / Q000032:analysis; D011485:Protein Binding; D011817:Rabbits; D012156:Reticulocytes / Q000032:analysis; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D012995:Solubility; D014508:Urea; D014981:Xenopus
D001798:Blood Proteins; D006146:Guanidines; D012269:Ribosomal Proteins; D014508:Urea; D008094:Lithium