Title: Fractionation of Rat‐Liver‐Chromatin Nonhistone Proteins into Two Groups with Different Metabolic Rates
Abstract: In the pH interval 10.5–11.8, 70% of the nonhistone proteins normally present in rat liver chromatin were dissociated. The rest remained complexed with DNA even at pH 13. Dodecylsulfate‐polyacrylamide gel electrophoresis revealed that the majority of the high‐molecular‐weight nonhistone proteins together with a few characteristic fractions with molecular weights of 40000–60000 remained in the alkali‐resistant group. l ‐[ 14 C]Leucine pulse‐labelling experiments showed that the specific radioactivity of the alkalilabile nonhistone proteins was 2–3 times higher than that of the alkali‐resistant nonhistone proteins, which, in turn, had the same specific radioactivity as that of the histones. The same held true for chromatin from regenerating rat liver. In the course of a 21‐day chase the specific radioactivity of the alkali‐labile nonhistone proteins gradually decreased and finally became 3 times lower than that of the alkali‐resistant nonhistone proteins. On the contrary, the ratio of the specific radioactivities of the alkali‐resistant nonhistone proteins and of the histones to the specific radioactivity of DNA remained constant during the chase. A conclusion can be drawn that a fraction of liver nonhistone proteins exists which is alkali‐resistant and is conserved in chromatin like histones.
Publication Year: 1975
Publication Date: 1975-10-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
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Cited By Count: 19
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