In previous communications (1, 2) we have presented evidence that rat liver mitochondria, when isolated under rigorously controlled conditions, retain their capacity for oxidative phosphorylation after treatments generally considered to be highly detrimental. In particular, a study was described of
Interaction of doxorubicin with nuclei isolated from rat liver and kidney
β Scribed by Tetsuya Terasaki; Tatsuji Iga; Yuichi Sugiyama; Manabu Hanano
- Publisher
- John Wiley and Sons
- Year
- 1984
- Tongue
- English
- Weight
- 547 KB
- Volume
- 73
- Category
- Article
- ISSN
- 0022-3549
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The development of hepatocyte polyploidy in rats aged up to 4 months was analyzed by flow cytometry using both scatter and fluorescent parameters to distinguish DNA diploid and DNA tetraploid populations and to discriminate between parenchymal and non-parenchymal compartments. The precise origin of
The fluorimetric measurement of DNA at levels of 0. I-1.0 fig in cytoplasmic fractions of rat liver is described. The DNA was quantitatively precipitated from the cytoplasm derived from as little as 10 mg of liver with cetyl trimethyl ammonium bromide (CTAB) and the fluorescence produced after react
This is a report of the changes during the first weeks of life of the rat in the concentration of three oxidases of kidney and liver. The study was made practicable by the availability of new analytical methods for these enzymes which require but a few milligrams of tissue per analysis (Burch et al.
Cluconeogenesis and palmitate incorporation into triacylglycerols and phosphatidylcholine were measured in isolated hepatocytes from control and ethanol-treated rats. Basal gluconeogenesis and its hormonal response decreased in hepatocytes from ethanol-treated animals; palmitate incorporation into t
## Abstract Mitochondrial ATPase from rat liver mitochondria contains multiple nucleotide binding sites. At low concentrations ADP binds with high affinity (1 mole/mole ATPase, K~D~ = 1β2 ΞΌM). At high concentrations, ADP inhibits ATP hydrolysis presumably by competing with ATP for the active site (