Author:
Gronow M,Thackrah T M,Lewis F A
Abstract
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.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
3 articles.
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1. Studies on the degradation of HeLa non-histone proteins;Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis;1980-01
2. Alkaline Hydrolysis of Nuclear Proteins;Biochemical Society Transactions;1979-02-01
3. The Use of Isoelectric Focusing in the Separation and Characterization of Nuclear Nonhistone Proteins;Biological and Biomedical Applications of Isoelectric Focusing;1977