INTRACELLULAR DISTRIBUTION OF DESOXYRIBONUCLEO-DEPOLYMERASE IN NORMAL RAT LIVER, LIVER TUMOR, AND LIVER OF ANIMALS FED p-DIMETHYLAMINOAZOBENZENE

1954 ◽  
Vol 32 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Gaston de Lamirande ◽  
Claude Allard ◽  
Antonio Cantero
Keyword(s):  
Rat Liver ◽  
Liver Tumor ◽  
Cell Activity ◽  
Mitotic Rate ◽  
Intracellular Distribution ◽  
Nuclear Fraction ◽  
Normal Rat ◽  
High Level ◽  
Soluble Material

The intracellular distribution of desoxyribonucleodepolymerase (DNase) has been investigated in the liver of animals fed p-dimethylaminoazobenzene (DAB), in liver freed from tumor, and in DAB induced tumor. The method is based on the determination of acid soluble material containing phosphorus, liberated by the action of the enzyme upon highly polymerized DNA. Results indicated that the nuclear DNase particularly accounts for a very low percentage of the whole cell activity in normal rat liver, whereas in nuclei of liver of DAB fed rats and of tumor the activity is increased to a high level. These facts suggest a possible correlation between the activity of DNase in the nuclear fraction and the mitotic rate of the tissue.

INTRACELLULAR DISTRIBUTION OF DESOXYRIBONUCLEO-DEPOLYMERASE IN NORMAL RAT LIVER, LIVER TUMOR, AND LIVER OF ANIMALS FED p-DIMETHYLAMINOAZOBENZENE

1954 ◽  
Vol 32 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Gaston de Lamirande ◽  
Claude Allard ◽  
Antonio Cantero
Keyword(s):  
Rat Liver ◽  
Liver Tumor ◽  
Cell Activity ◽  
Mitotic Rate ◽  
Intracellular Distribution ◽  
Nuclear Fraction ◽  
Normal Rat ◽  
High Level ◽  
Soluble Material

The intracellular distribution of desoxyribonucleodepolymerase (DNase) has been investigated in the liver of animals fed p-dimethylaminoazobenzene (DAB), in liver freed from tumor, and in DAB induced tumor. The method is based on the determination of acid soluble material containing phosphorus, liberated by the action of the enzyme upon highly polymerized DNA. Results indicated that the nuclear DNase particularly accounts for a very low percentage of the whole cell activity in normal rat liver, whereas in nuclei of liver of DAB fed rats and of tumor the activity is increased to a high level. These facts suggest a possible correlation between the activity of DNase in the nuclear fraction and the mitotic rate of the tissue.

scholarly journals Intracellular Distribution of 5' Nucleotidase in Rat Liver

1958 ◽  
Vol 4 (4) ◽  
pp. 373-376 ◽  
Author(s):  
Gaston de Lamirande ◽  
Claude Allard ◽  
Antonio Cantero
Keyword(s):  
Enzymatic Activity ◽  
Rat Liver ◽  
Biochemical Analysis ◽  
Inorganic Phosphorus ◽  
Intracellular Distribution ◽  
Differential Centrifugation ◽  
Nucleotidase Activity ◽  
Rat Liver Cells ◽  
Cell Fractions

The intracellular distribution of 5' nucleotidase was investigated in rat liver by biochemical analysis of cell fractions obtained by differential centrifugation. The enzymatic activity was measured by determination of the inorganic phosphorus liberated from 5' nucleotides. The 5' nucleotidase activity was mainly found in the nuclear and microsomal fractions. An attempt to extract the enzyme from these fractions with Mg++ ion solutions was unsuccessful. It is concluded that 5' nucleotidase is actually present in the nuclear and microsomal fractions of rat liver cells.

Intracellular Distribution of Acid and Alkaline Ribonuclease in Normal Rat Liver

Science ◽  
1954 ◽  
Vol 119 (3089) ◽  
pp. 351-353 ◽  
Author(s):  
G. de Lamirande ◽  
C. Allard ◽  
H. C. da Costa ◽  
A. Cantero
Keyword(s):  
Rat Liver ◽  
Intracellular Distribution ◽  
Normal Rat ◽  
Alkaline Ribonuclease

Experimental determination of threshold dose in photodynamic therapy in normal rat liver

2007 ◽  
Vol 4 (6) ◽  
pp. 469-475 ◽  
Author(s):  
J Ferreira ◽  
L T Moriyama ◽  
C Kurachi ◽  
C Sibata ◽  
O Castro e Silva Jr. ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Experimental Determination ◽  
Rat Liver ◽  
Threshold Dose ◽  
Normal Rat

scholarly journals Partial purification of a 6-methyladenine mRNA methyltransferase which modifies internal adenine residues

1992 ◽  
Vol 288 (1) ◽  
pp. 233-240 ◽  
Author(s):  
M T Tuck
Keyword(s):  
Rat Liver ◽  
Rat Kidney ◽  
Cell Activity ◽  
Deae Cellulose ◽  
Enzymic Activity ◽  
Partial Purification ◽  
Methyltransferase Activity ◽  
Nuclear Extracts ◽  
Normal Rat ◽  
Minor Form

Two forms of a 6-methyladenine mRNA methyltransferase have been partially purified using a T7 transcript coding for mouse dihydrofolate reductase as an RNA substrate. Both enzyme forms modify internal adenine residues within the RNA substrate. The enzymes were purified 357- and 37-fold respectively from nuclear salt extracts prepared from HeLa cells using DEAE-cellulose and phosphocellulose chromatography. The activity of the first form of the enzyme eluted from DEAE-cellulose (major form) was at least 3-fold greater than that of the second (minor form). H.p.l.c. analysis of the hydrolysed, methylated mRNA substrates demonstrated that both forms of the enzyme produced only 6-methyladenine. The two forms of the enzyme differed in their RNA substrate specificity as well as in the dependence for a 5′ cap structure. The 6-methyladenine mRNA methyltransferase activity was found to be elevated in HeLa nuclei as compared with nuclear extracts from rat kidney and brain. Enzymic activity could not be detected in nuclei from either normal rat liver or regenerating rat liver. In the case of the HeLa cell, activity could only be detected in nuclear extracts, with a small amount in the ribosomal fraction. Other HeLa subcellular fractions were void of activity.

BINDING OF CORTICOSTERONE IN RAT LIVER

1970 ◽  
Vol 47 (2) ◽  
pp. 149-158 ◽  
Author(s):  
R. S. SNART ◽  
N. N. SANYAL ◽  
M. K. AGARWAL
Keyword(s):  
Rat Liver ◽  
Binding Sites ◽  
Microsomal Fraction ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Gel Filtration ◽  
Nuclear Fraction ◽  
Binding Characteristics ◽  
Mole Percentage

SUMMARY The binding characteristics of corticosterone by rat liver were studied by a displaceable binding technique. The binding of corticosterone to protein fractionated by gel filtration and density gradient centrifugation has been carried out as a preliminary determination of the nature of the binding sites. The results were analysed and showed three types of binding sites for corticosterone with the characteristic association constants at 0° of K1 = 1·2 × 1010, K2 = 1 × 108 and K3 = 1 × 104 1./mole. Percentage displacement of corticosterone from the nuclear fraction did not differ significantly from that from tissue or the mitochondrial-microsomal fraction. The K1 and K2 sites persisted in separated buffer-soluble fractions but were destroyed on mild heating leaving only the K3 sites.

scholarly journals INTRACELLULAR DISTRIBUTION OF ALKALINE PHOSPHATASE IN RAT LIVER CELLS

1955 ◽  
Vol 1 (4) ◽  
pp. 315-330 ◽  
Author(s):  
Arthur J. Emery ◽  
Alexander L. Dounce
Keyword(s):  
Alkaline Phosphatase ◽  
Rat Liver ◽  
Nuclear Membrane ◽  
Aqueous Media ◽  
Isotonic Saline ◽  
Intracellular Distribution ◽  
Supernatant Fraction ◽  
Nuclear Fraction ◽  
Modified Method ◽  
Soluble Supernatant

1. Cytochemical studies of the intracellular distribution of alkaline phosphatase in rat liver have been made, using a fractionation procedure recently developed in this laboratory (8) and a similar but modified method not described previously. Aqueous media were used in both cases. 2. The alkaline phosphatase was found to consist of two forms, one of which is strongly activated by magnesium and one of which is not sensitive to this metal. 3. The form of the enzyme that is not activated by magnesium occurs mainly in the nuclear fraction, where it seems to be rather firmly bound. Some of this form of the enzyme is also found in the microsomes, but very little if any occurs in the soluble supernatant fraction. 4. The form of alkaline phosphatase which is activated by magnesium occurs mainly in the soluble supernatant fraction, but what is believed are significant amounts also occur in nuclei. A significant portion of this form of the enzyme can be extracted from the isolated nuclei with cold, isotonic saline solution. Some activity of this form of the enzyme is also found in the microsomal fraction. 5. Mitochondria appear to contain relatively little alkaline phosphatase of either kind. 6. The concept of a porous nuclear membrane has been invoked to explain some of the results obtained in this work. It is postulated that part at least of the form of the enzyme that is activated by magnesium is free to diffuse back and forth through pores in the nuclear membrane, whereas this is considered not to be possible for the form of the enzyme that is insensitive to magnesium as a result of the firm binding of the latter to nuclear substance.

scholarly journals STUDIES ON THE FUNCTION OF INTRACELLULAR RIBONUCLEASES

1966 ◽  
Vol 29 (3) ◽  
pp. 387-393 ◽  
Author(s):  
Takeshi Utsunomiya ◽  
Jay S. Roth
Keyword(s):  
Rat Liver ◽  
Lipid Content ◽  
Growth Rates ◽  
Degradation Products ◽  
Normal Liver ◽  
Intracellular Distribution ◽  
High Lipid Content ◽  
High Lipid ◽  
Normal Rat

Polysome and ribosome preparations from normal rat liver and from a series of transplantable rat hepatomas of different growth rates were compared. All the hepatomas had a significantly higher percentage of RNA in a polysome preparation than did the normal liver, and the polysome preparations from the tumors, with the exception of the Dunning hepatoma which has a high lipid content, gave a greater yield of RNA and protein per gram of wet tissue than the liver did. Heavier polysomes were considerably less prevalent in the tumors than in the liver, and the tumors contained a larger proportion of monomer and dimer ribosomes than the liver did. Evidence is presented that the increased monomer and dimer ribosome population of the hepatomas studied is not an artifact of preparation, but represents the true intracellular distribution. Ribosomes from normal liver and Morris 5123-D hepatoma were readily dissociated by 20 min' treatment with 1.0 mM EDTA, but ribosomes from the Dunning, Novikoff ascites, and McCoy MDAB hepatomas were little affected by such treatment. With higher concentrations of EDTA, the ribosomes from the Novikoff ascites and McCoy MDAB hepatomas broke down and did not form specific subunits as did ribosomes from liver and the Morris 5123-D hepatoma but rather gave rise to a variety of small degradation products. This behavior is ascribed to a higher RNase content of the Novikoff and McCoy MDAB hepatomas. Dunning hepatoma ribosomes were resistant to 4 mM EDTA.

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