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Abstract ▼ AI-Helper

SDS gel electrophoresis has been employed to examine the changes in distribution of three major classes of nuclear proteins extracted from isolated liver nuclei in response to refeeding of starved rats with a fat-free high carbohydrate diet and following insulin injection into streptozotocin-diabeti...

SDS gel electrophoresis has been employed to examine the changes in distribution of three major classes of nuclear proteins extracted from isolated liver nuclei in response to refeeding of starved rats with a fat-free high carbohydrate diet and following insulin injection into streptozotocin-diabetic rats. The relative quantity of electrophoretically separated proteins in the fraction showed marked changes with 0.14 NaCl extracts, but not with histones and phenol soluble non-histone proteins. During 48h starvation at least five proteins ranging in molecular weight from 50,000 to 180,000 daltons decreased relative to normal controls while a protein with 36,000 daltons was increased. Refeeding the starved rats with a high carbohydrate diet reversed these changes over 24 h. Insulin injection into streptozotocin-diabetic rats increased levels of the set of five 0.14 M NaCl soluble proteins identified from refeeding experiment of starved rats. The 36,000 daltons protein was also diminished. These results indicate that changes in distribution of certain nuclear proteins in 0.14M NaCl extracts are associated with the control of nuclear activity ralated to known insulin-signalled modulation and induction of cytosolic lipogenic enzymes.