Properties of Adlehyde Dehydrogenase from Chemically-Induced Rat Hepatomas and Normal Rat Liver

1980 ◽  
pp. 85-93
Author(s):  
Ronald Lindahl
Keyword(s):  
Rat Liver ◽  
Chemically Induced ◽  
Normal Rat

scholarly journals STUDIES ON THE FUNCTION OF INTRACELLULAR RIBONUCLEASES

1966 ◽  
Vol 29 (3) ◽  
pp. 395-403 ◽  
Author(s):  
Takeshi Utsunomiya ◽  
Jay S. Roth
Keyword(s):  
Natural Products ◽  
Sodium Chloride ◽  
Rat Liver ◽  
Messenger Rna ◽  
Rnase Activity ◽  
Optimum Ph ◽  
Normal Rat ◽  
Pancreatic Rnase ◽  
The Stability ◽  
Normal Constituent

The RNase activity and properties of ribosome and polysome preparations from normal rat liver and some hepatomas have been examined. Polysome and ribosome preparations from the Novikoff, McCoy MDAB, and Dunning hepatomas had considerably higher specific RNase activity than corresponding preparations from normal rat liver, Novikoff ascites, or Morris 5123 hepatomas. The optimum pH of the RNase was approximately 8.5 for all samples tested, and the samples showed no evidence of latent RNase activity when treated with 3 M sodium chloride, EDTA, urea, or p-chloromercuribenzenesulfonic acid. The RNase activity appeared to be associated principally with breakdown products and/or subunits smaller than 80S. In the presence of Mg++ ions, subunits could reaggregate to form monomer ribosomes indistinguishable from the natural products, but some of the reassociated ribosomes could contain RNase activity which had been bound to the smaller particles. Similar results were obtained with spermine. In the hepatomas, evidence was obtained for the preexistence of considerable amounts of the smaller, RNase-containing subunits in the cell. When a small amount of crystalline bovine pancreatic RNase was added to partly dissociated ribosomes, the RNase was found only in association with the smaller subunits, and little or no enzyme was taken up by ribosomes or polysomes. The results have led to the conclusion that RNase is not a normal constituent of the ribosome or polysome, but that RNase may become associated with these particulates if dissociation and reassociation take place. Some implications of these findings for the stability of messenger RNA and for the mechanism of its breakdown are discussed.

Intracellular re-localisation by photochemical internalisation enhances the cytotoxic effect of gelonin — Quantitative studies in normal rat liver

2010 ◽  
Vol 142 (3) ◽  
pp. 347-353 ◽  
Author(s):  
Josephine Woodhams ◽  
Pei-Jen Lou ◽  
Pål K. Selbo ◽  
Alexander Mosse ◽  
Dahmane Oukrif ◽  
...  
Keyword(s):  
Rat Liver ◽  
Cytotoxic Effect ◽  
Quantitative Studies ◽  
Normal Rat

scholarly journals Retinyl palmitate hydrolase activity in normal rat liver.

1981 ◽  
Vol 256 (9) ◽  
pp. 4498-4503
Author(s):  
J.H. Prystowsky ◽  
J.E. Smith ◽  
D.S. Goodman
Keyword(s):  
Rat Liver ◽  
Retinyl Palmitate ◽  
Hydrolase Activity ◽  
Normal Rat

Hepatoma, host liver, and normal rat liver phospholipids as affected by diet

Lipids ◽  
1975 ◽  
Vol 10 (12) ◽  
pp. 736-745 ◽  
Author(s):  
Randall Wood
Keyword(s):  
Rat Liver ◽  
Host Liver ◽  
Normal Rat

scholarly journals Subcellular localization of DNA-binding protein BA by immunofluorescence and immunoelectron microscopy

1979 ◽  
Vol 83 (2) ◽  
pp. 462-463 ◽  
Author(s):  
JJ Catino ◽  
H Busch ◽  
Y Daskal ◽  
LC Yeoman
Keyword(s):  
Immunoelectron Microscopy ◽  
Rat Liver ◽  
Human Lymphocytes ◽  
Chromosomal Protein ◽  
Nonhistone Protein ◽  
Quiescent Cells ◽  
Normal Rat ◽  
Normal Human ◽  
Antigen Localization ◽  
Relationship Of

Nonhistone protein BA has been shown to decrease in amount in the chromatin of growth- stimulated normal rat liver (Yeoman et al. 1975. Cancer Res. 35:1249-1255) and in mitogen-stimulated normal human lymphocytes (Yeoman et al. 1976. Exp. Cell Res. 100:47- 55.). Subsequently, protein BA was purified and was shown to prefer to bind to double- stranded A-T-rich DNAs (Catino et al. 1978. Biochemistry. 17:983-987.). Immunization of rabbits with highly purified protein BA has resulted in the production of a specific antibody. A specific immunoreactivity for chromosomal protein BA has been demonstrated by immunoelectrophoresis and double antibody immunoprecipitation analysis with rabbit anti-BA immunoglobulin and IgG fractions. Light microscope examination of normal rat liver crysections by the indirect immunofluorescence procedure has demonstrated a cytoplasmic as well as a nuclear localization for protein BA with a pronounced perinucleolar fluorescence. Immunoelectron microscopy employing the peroxidase antiperoxidase method of antigen localization has confirmed the immunofluorescence data and has show a heterochromatin localization for protein BA. The relationship of the localization of protein BA to gene control in quiescent cells or to configurations of heterochromatin as well as the marked reduction in the amounts of protein BA which occur in stimulated growth states remains to be defined.

Effect of Aureomycin on the Respiration of Normal Rat Liver Homogenates

Science ◽  
1951 ◽  
Vol 113 (2932) ◽  
pp. 273-273
Author(s):  
J. C. Van Meter ◽  
J. J. Oleson
Keyword(s):  
Rat Liver ◽  
Normal Rat ◽  
Liver Homogenates

scholarly journals Properties of cytosolic components activating rat hepatic 5-deiodination in the presence of NADPH

1986 ◽  
Vol 234 (2) ◽  
pp. 391-398 ◽  
Author(s):  
K Sawada ◽  
B C W Hummel ◽  
P G Walfish
Keyword(s):  
Enzyme Activity ◽  
Glutathione Reductase ◽  
Rat Liver ◽  
Column Chromatography ◽  
Reduced Glutathione ◽  
Hydrogen Acceptor ◽  
Simultaneous Addition ◽  
Heat Stable ◽  
Hepatic Microsomes ◽  
Normal Rat

The effects of cytosol, NADPH and reduced glutathione (GSH) on the activity of 5′-deiodinase were studied by using washed hepatic microsomes from normal fed rats. Cytosol alone had little stimulatory effect on the activation of microsomal 5′-deiodinase. NADPH had no stimulatory effect on the microsomal 5′-deiodinase unless cytosol was added. 5′-deiodinase activity was greatly enhanced by the simultaneous addition of NADPH and cytosol (P less than 0.001); this was significantly higher than that with either NADPH or cytosol alone (P less than 0.001). GSH was active in stimulating the enzyme activity in the absence of cytosol, but the activity of 5′-deiodinase with 62 microM-NADPH in the presence of cytosol was significantly higher than that with 250 microM-GSH in the presence of the same concentration of cytosol (P less than 0.001). The properties of the cytosolic components essential for the NADPH-dependent activation of microsomal 5′-deiodinase independent of a glutathione/glutathione reductase system were further assessed using Sephadex G-50 column chromatography to yield three cytosolic fractions (A, B and C), wherein A represents pooled fractions near the void volume, B pooled fractions of intermediate Mr (approx. 13 000), and C of low Mr (approx. 300) containing glutathione. In the presence of NADPH (1 mM), the 5′-deiodination rate by hepatic washed microsomes is greatly increased if both A and B are added and is a function of the concentrations of A, B, washed microsomes and NADPH. A is heat-labile, whereas B is heat-stable and non-dialysable. These observations provide the first evidence of an NADPH-dependent cytosolic reductase system not involving glutathione which stimulates microsomal 5′-deiodinase of normal rat liver. The present data are consistent with a deiodination mechanism involving mediation by a reductase (other than glutathione reductase) in fraction A of an NADPH-dependent reduction of a hydrogen acceptor in fraction B, followed by reduction of oxidized microsomal deiodinase by the reduced acceptor (component in fraction B).

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