Study of mammalian ribosomal protein reactivity in situ. II. - Effect of glutaraldehyde and salts.
Results concerning ribosomal protein sensitivity to glutaraldehyde were compared to protein depletion studies using LiCl centrifugation. The relative degree of reactivity of the different proteins was determined by two-dimensional acrylamide gel electrophoresis, and the activity of the reacted subunits was measured. The results obtained mostly confirmed the studies of methoxynitrotropone reactivity reported earlier. For example, L16, L25, L29, L30, L31, S18, S20 appeared to be definitely exposed to both NH2-reagents and LiCl. Some interesting points emerged from this study regarding protein topography in both subunits: (1) with few exceptions, almost all ribosomal proteins were accessible to the surrounding medium; (2) the sensitivity of the 40S proteins to the three reagents used was lower than was that of the 60S proteins; (3) the reactivities of the subunit components changed when subunits were associated: L8 was more reactive with glutaraldehyde in 60S subunits than in 80S ribosomes. In contrast, S14, S15 and S19 were more exposed in ribosomes than in the 40S subunits.
D000447:Aldehydes; D000818:Animals; D002498:Centrifugation; D055598:Chemical Phenomena; D002621:Chemistry; D003864:Depression, Chemical; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D005976:Glutaral / Q000494:pharmacology; D008094:Lithium / Q000494:pharmacology*; D008099:Liver; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D051381:Rats; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000187:drug effects*; D013329:Structure-Activity Relationship
D000447:Aldehydes; D012269:Ribosomal Proteins; D008094:Lithium; D005976:Glutaral