Occurrence of histone-related oxalate binding in rat liver nucleus

1996 ◽  
Vol 156 (2) ◽  
pp. 93-100 ◽  
Author(s):  
Ramasamy Selvam ◽  
Vadlamudi Prasanna Lakshmi
Keyword(s):  
Rat Liver ◽  
Liver Nucleus

scholarly journals Hemoglobin Formation in the Rat Liver Nucleus.

1955 ◽  
Vol 9 ◽  
pp. 1045-1045 ◽  
Author(s):  
R. Bonnichsen ◽  
G. Hevesy ◽  
John Glomset ◽  
Albertina Caglieris
Keyword(s):  
Rat Liver ◽  
Liver Nucleus

Differential Effects of Growth Hormone and Hydrocortisone on Nuclear RNA Synthesis in Rat Liver

1971 ◽  
Vol 49 (7) ◽  
pp. 853-862 ◽  
Author(s):  
Peter M. K. Ip ◽  
Maurice Brossard
Keyword(s):  
Growth Hormone ◽  
Rat Liver ◽  
Rna Synthesis ◽  
Present Report ◽  
Liver Nucleus ◽  
Double Labeling ◽  
Nuclear Rna Synthesis ◽  
Nuclear Rna ◽  
Liver Nuclei ◽  
Nucleolar Rna

RNA has been isolated and fractionated from rat liver nuclei by a sequence of salt extractions into four subfractions: namely nucleoplasmic, deoxyribonucleoprotein-associated, ribonucleoprotein-associated, and nucleolar fractions.Study of 14C-methyl-methionine labeling indicates that the nucleolar RNA fraction isolated by the present procedure is, in fact, of nucleolar origin while the other three fractions are essentially of extranucleolar origin.The effects of growth hormone and hydrocortisone on the nuclear RNA synthesis have been further studied using the present isolation and double-labeling techniques. Both hormones cause an increase in the incorporation of labeled orotic acid into all types of RNA in all four nuclear subfractions. However, the stimulatory effect of growth hormone is found mainly in the 18–28 S and 45–60 S regions of the nucleolar fraction and in regions of the entire gradient of the nucleoplasmic fraction, whereas the stimulatory effect of hydrocortisone is localized mainly in the 10–28 S regions of the nucleolar fraction and in the 4 S and 10–18 S regions of the ribonucleoprotein fraction.The present report suggests that there are qualitative as well as quantitative differences in the action of growth hormone and hydrocortisone on the synthesis of RNA in liver nucleus. The mode of action of the two hormones is discussed.

scholarly journals Detoxification of DNA hydroperoxide by glutathione transferases and the purification and characterization of glutathione transferases of the rat liver nucleus

1988 ◽  
Vol 254 (3) ◽  
pp. 841-845 ◽  
Author(s):  
K H Tan ◽  
D J Meyer ◽  
N Gillies ◽  
B Ketterer
Keyword(s):  
Rat Liver ◽  
Peroxidase Activity ◽  
Glutathione Transferases ◽  
Supernatant Fraction ◽  
Liver Nucleus ◽  
Purification And Characterization ◽  
Soluble Supernatant

DNA peroxidized by exposure to ionizing radiation in the presence of oxygen is a substrate for the Se-independent GSH peroxidase activity of several GSH transferases, GSH transferases 5-5, 3-3 and 4-4 being the most active in the rat liver soluble supernatant fraction (500, 35 and 20 nmol/min per mg of protein respectively) and GSH transferases mu and pi the most active, so far found, in the human liver soluble supernatant fraction (80 and 10 nmol/min per mg respectively). Although the GSH transferase content of the rat nucleus was found to be much lower than that of the soluble supernatant, nuclear GSH transferases are likely to be more important in the detoxification of DNA hydroperoxide produced in vivo. Two nuclear fractions were studied, one extracted with 0.075 M-saline/0.025 M-EDTA, pH 8.0, and the other extracted from the residue with 8.5 M-urea. The saline/EDTA fraction contained subunits 1, 2, 3, 4 and a novel subunit, similar but not identical to 5, provisionally referred to as 5*, in the proportions 40:25:5:5:25 respectively. The 8.5 M-urea-extracted fraction contained principally subunit 5* together with a small amount of subunit 6 in the proportion 95:5 respectively. GSH transferase 5*-5* purified from the 8.5 M-urea extract has the highest activity towards DNA hydroperoxide of any GSH transferase so far studied (1.5 mumol/min per mg). A Se-dependent GSH peroxidase fraction from rat liver was also active towards DNA hydroperoxide; however, since this enzyme accounts for only 14% of the GSH peroxidase activity detectable in the nucleus, GSH transferases may be the more important source of this activity. The possible role of GSH transferases, in particular GSH transferase 5*-5*, in DNA repair is discussed.

Replacing dietary glucose with fructose increases ChREBP activity and SREBP-1 protein in rat liver nucleus

2009 ◽  
Vol 390 (2) ◽  
pp. 285-289 ◽  
Author(s):  
Hyun-Young Koo ◽  
Michio Miyashita ◽  
B.H. Simon Cho ◽  
Manabu T. Nakamura
Keyword(s):  
Rat Liver ◽  
Liver Nucleus
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