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M S Moruzzi

Publications and source records attributed to M S Moruzzi.

At least 37 records · Page 2Linked to original sources
PubMed1975

Modification of the template capacity of liver chromatin for form-B ribonucleic acid polymerase by food intake in rats under controlled feeding schedules.

Nuclei from liver of rats accustomed to eating during the first 8h of a daily 12h dark period demonstrate an increased capacity to synthesize RNA 6H after the beginning of the feeding period. 2. This increase is accompanied by a higher yield of extractable form-B DNA-dependent RNA polymerase activity. 3. The endogenous RNA polymerase activity associated with nuclear chromatin is also stimulated by food intake. Both purified and chromatin-associated form-B enzyme activities exhibit different ionic strength requirements after food intake. 4. The sensitivity of exogenous (added) form-B-enzyme to changes in ionic strength changes after feeding when chromatin is used as template. 5. Chromatin extracted from the liver of fed rats is a better template for form-B-enzyme than chromatin extracted from starved rats.

Ammonium Sulfate↗
PubMed1975

The effect of spermine on transcription of mammalian chromatin by mammalian deoxyribonucleic acid-dependent ribonucleic acid polymerase.

Isolated rat liver nuclei demonstrate an increased ability to synthesize RNA in the presence of either spermine or spermidine. Spermidine has more effect on the low-salt alpha-amanitin-insensitive reaction, and spermine has more effect on the high-salt alpha-amanitin-sensitive reaction. Spermine is effective at concentrations of 0.1 mM and 1 muM, showing a biphasic effect. The RNA polymerase activity associated with nuclear chromatin is increased in the presence of spermine only at a concentration of 0.1 mM. Aso the transcription of deproteinized liver DNA by liver form-B polymerase or Escherichia coli enzyme is more efficient in the presence of 0.1 mM-spermine. Only when liver chromatin is transcribed by its homologous enzyme (and not by E. coli enzyme) is spermine active at both 0.1mM and 1 muM as in purified nuclei. The lower concentration of spermine (1 muM) is able to affect chromatin transcription by increasing the affinity of chromatin for the enzyme. Our findings suggest a regulatory role of spermine at the level of genome transcription.

Amanitins↗