Instability of rat liver chromatin and other nuclear non-histone proteins in alkaline solution.
Non-histone proteins from rat liver nuclei and chromatin were shown to be hydrolysed in 0.1M or-1M-NaOH solutions both at 4 degrees and 18 degrees C; 24h in 1M-NaOH at 18 degrees C is sufficient to break down approx. 77% of these proteins to low-molecular-weight peptides. Loss of protein material banding in the region of pH5.5-8.0 has been demonstrated by isoelectric focusing in polyacrylamide gels, and fine high-molecular-weight bands are no longer visible on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The results indicate that care must be taken when analysing non-histone-protein fractions to avoid exposure to alkaline pH conditions.
D000818:Animals; D002843:Chromatin / Q000032:analysis*; D006868:Hydrolysis; D008099:Liver / Q000032:analysis; D008970:Molecular Weight; D009698:Nucleoproteins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D012972:Sodium Hydroxide
D002843:Chromatin; D009698:Nucleoproteins; D010446:Peptide Fragments; D012972:Sodium Hydroxide