Studies on in vitro RNA Synthesis by RNA Polymerases from Rat Liver Tissue

1973 ◽  
pp. 139-162 ◽  
Author(s):  
K. H. Seifart ◽  
A. Ferencz ◽  
B. Benecke
Keyword(s):  
Rat Liver ◽  
Liver Tissue ◽  
Rna Synthesis ◽  
Rna Polymerases

Effect of Prolonged Consumption of Pemmican Survival Ration on Some Aspects of the Intermediary Metabolism of Rat Liver Tissue

1958 ◽  
Vol 193 (2) ◽  
pp. 449-454 ◽  
Author(s):  
John P. Hannon ◽  
David A. Vaughan
Keyword(s):  
Cytochrome C ◽  
Respiratory Rate ◽  
Rat Liver ◽  
Liver Tissue ◽  
In Vitro Metabolism ◽  
Intermediary Metabolism ◽  
Normal Value ◽  
Endogenous Metabolism ◽  
Prolonged Feeding

The effect of prolonged feeding (3–5 months) of pemmican on some aspects of the in vitro metabolism of liver tissue was investigated. The endogenous metabolism of liver slices and homogenates was significantly increased by pemmican, probably due to an increase in the amount of readily metabolizable substrate. Utilizing mitochondrial preparations, it was found that with all substrates studied, except glutamate, α-ketoglutarate and succinate, the respiratory rate was not affected by the previous diet in the absence of added cytochrome c and diphosphopyridine nucleotide. The three substrates mentioned were oxidized at significantly lower rates in the pemmican group. Upon the addition of cytochrome c and diphosphopyridine nucleotide the qo2 of glutamate, α-ketoglutarate, and succinate was returned to the normal value.

Different rates of glucose and fructose metabolism in rat liver tissue in vitro

Metabolism ◽  
1971 ◽  
Vol 20 (4) ◽  
pp. 392-400 ◽  
Author(s):  
J.N. Pereira ◽  
Norman O. Jangaard
Keyword(s):  
Rat Liver ◽  
Liver Tissue ◽  
Fructose Metabolism

Phosphorylation of RNA polymerases: specific association of protein kinase NIl with RNA polymerase I

1983 ◽  
Vol 302 (1108) ◽  
pp. 135-142 ◽  
Keyword(s):  
Protein Kinase ◽  
Rna Polymerase ◽  
Rna Synthesis ◽  
Rna Polymerase Iii ◽  
Rna Polymerases ◽  
Rna Polymerase I ◽  
Liver Protein ◽  
Protein Kinase N ◽  
Polymerase I

The activities of the three DNA-dependent RNA polymerases from a rapidly growing rat tumour, Morris hepatoma 3924 A, and from rat liver were examined. The activity of RNA polymerase I was higher in the tumour than in the liver. The enhanced capacity for RNA synthesis was a result of a higher concentration of polymerase I in the tumour as well as of an activation of this enzyme vivo. The possibility that the high specific activity of the hepatoma polymerase I resulted from phosphorylation was investigated. Two major cyclic-AMP-independent nuclear casein kinases (NI and N il) were identified; the activity of protein kinase N il in the tumour was ten times that in liver. Protein kinase N il was capable of activating and phosphorylating RNA polymerase I in vitro . This kinase could also stimulate RNA polymerase II activity, although to a lesser extent than RNA polymerase I. RNA polymerase III was not affected by protein kinase NIL Protein kinase N il was tightly associated with polymerase I and was found even in purified preparations of the polymerase. Antibodies against both RNA polymerase I and protein kinase N il were present in sera of patients with certain rheumatic autoimmune diseases. These results imply that RNA polymerase I and protein kinase NIl are in close association in vivo as well as in vitro and that polymerase phosphorylation may regulate the rate of ribosomal RNA synthesis in the cell.

The Effect of Thyroid Hormone on in Vitro Rat Liver Mitochondrial RNA Synthesis

Endocrinology ◽  
1977 ◽  
Vol 100 (1) ◽  
pp. 52-60 ◽  
Author(s):  
CHARLES P. BARSANO ◽  
LESLIE J. DEGROOT ◽  
GODFREY S. GETZ
Keyword(s):  
Thyroid Hormone ◽  
Rat Liver ◽  
Rna Synthesis ◽  
Mitochondrial Rna
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