scholarly journals Growth of liver accompanied by an increased binding of aminoacyl-transfer ribonucleic acids

1977 ◽  
Vol 166 (3) ◽  
pp. 463-471 ◽  
Author(s):  
D McEwen Nicholls ◽  
J Carey ◽  
W Sendecki
Keyword(s):  
Rat Liver ◽  
Inhibitory Activity ◽  
Elongation Factor ◽  
Supernatant Fraction ◽  
Regenerating Liver ◽  
Ribosomal Subunits ◽  
Ribonucleic Acids ◽  
Aminoacyl Transfer ◽  
Elongation Factor 1 ◽  
Trna Binding

Homogenates of rat liver obtained 3 or 14 days after partial hepatectomy were used to prepare the postmicrosomal pH5-supernatant fraction and to prepare salt-wash fractions of the 40S ribosomal subunits and the 80S ribosomes. The factor-dependent binding of methionyl-tRNAfMet to ribosomes and the elongation-factor-1-dependent binding of phenylalanyl-tRNA to ribosomes were both increased after 3 days of growth, but not after 14 days of growth. An activity inhibitory to phenylalanyl-tRNA binding that was located in ribosomal wash fractions was decreased after 14 days of growth. Since the decreased inhibitory activity was obtained from the ribosomes and was tested against ribosomes and excess of pH5-supernatant fraction from control rat liver, its action was separate from the phenylalanyl-tRNA binding activities of the pH5-supernatant fractions from sham-operated and regenerating liver.

scholarly journals Regeneration of renal proximal tubules after mercuric chloride injury is accompanied by increased binding of aminoacyl-transfer ribonucleic acid

1976 ◽  
Vol 160 (2) ◽  
pp. 357-365 ◽  
Author(s):  
D McEwen ◽  
K Ng
Keyword(s):  
Rat Kidney ◽  
Elongation Factor ◽  
Proximal Tubules ◽  
Supernatant Fraction ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Aminoacyl Transfer ◽  
Increased Activity ◽  
Elongation Factor 1 ◽  
Trna Binding

Homogenates of rat kidney cortex obtained 1,3 or 14 days after a single injection of HgCl2 were used to prepare the post-microsomal pH5 supernatant fraction. The activity of this fraction for peptide synthesis from [14C]phenylalanyl-tRNA was significantly increased at 1 and 3 days, at which time the proximal tubules are regenerating [Cuppage & Tate (1967) Am. J. Pathol. 51, 405-429]. This increased activity could not be attributed to a decreased inhibitory activity, but was due to an increased aminoacyl-tRNA binding, i.e. elongation-factor-1 activity, in the supernatant fraction.

scholarly journals tRNA binding stabilizes rat liver 60 S ribosomal subunits during treatment with LiCl.

1980 ◽  
Vol 255 (14) ◽  
pp. 6954-6961 ◽  
Author(s):  
A.M. Reboud ◽  
S. Dubost ◽  
M. Buisson ◽  
J.P. Reboud
Keyword(s):  
Rat Liver ◽  
Ribosomal Subunits ◽  
Trna Binding

Polypeptide elongation factor 1 and the control of elongation rate in rat liver in vivo

Nature ◽  
1976 ◽  
Vol 264 (5588) ◽  
pp. 804-806 ◽  
Author(s):  
JENNIFER B. K. NIELSEN ◽  
PATRICIA W. PLANT ◽  
AUDREY E. V. HASCHEMEYER
Keyword(s):  
Rat Liver ◽  
Elongation Factor ◽  
Elongation Rate ◽  
Elongation Factor 1

scholarly journals Inhibition of microsomal lipid peroxidation by glutathione and glutathione transferases B and AA. Role of endogenous phospholipase A2

1984 ◽  
Vol 220 (1) ◽  
pp. 243-252 ◽  
Author(s):  
K H Tan ◽  
D J Meyer ◽  
J Belin ◽  
B Ketterer
Keyword(s):  
Lipid Peroxidation ◽  
Phospholipase A2 ◽  
Rat Liver ◽  
Inhibitory Activity ◽  
Liver Microsomes ◽  
Supernatant Fraction ◽  
Rat Liver Microsomes ◽  
Microsomal Lipid Peroxidation ◽  
Soluble Supernatant

Lipid peroxidation in vitro in rat liver microsomes (microsomal fractions) initiated by ADP-Fe3+ and NADPH was inhibited by the rat liver soluble supernatant fraction. When this fraction was subjected to frontal-elution chromatography, most, if not all, of its inhibitory activity could be accounted for by the combined effects of two fractions, one containing Se-dependent glutathione (GSH) peroxidase activity and the other the GSH transferases. In the latter fraction, GSH transferases B and AA, but not GSH transferases A and C, possessed inhibitory activity. GSH transferase B replaced the soluble supernatant fraction as an effective inhibitor of lipid peroxidation in vitro. If the microsomes were pretreated with the phospholipase A2 inhibitor p-bromophenacyl bromide, neither the soluble supernatant fraction nor GSH transferase B inhibited lipid peroxidation in vitro. Similarly, if all microsomal enzymes were heat-inactivated and lipid peroxidation was initiated with FeCl3/sodium ascorbate neither the soluble supernatant fraction nor GSH transferase B caused inhibition, but in both cases inhibition could be restored by the addition of porcine pancreatic phospholipase A2 to the incubation. It is concluded that the inhibition of microsomal lipid peroxidation in vitro requires the consecutive action of phospholipase A2, which releases fatty acyl hydroperoxides from peroxidized phospholipids, and GSH peroxidases, which reduce them. The GSH peroxidases involved are the Se-dependent GSH peroxidase and the Se-independent GSH peroxidases GSH transferases B and AA.

scholarly journals Peptide elongation in rat kidney after cadmium administration

1980 ◽  
Vol 190 (3) ◽  
pp. 791-797 ◽  
Author(s):  
M J Kuliszewski ◽  
D M Nicholls
Keyword(s):  
Rat Kidney ◽  
Gel Filtration ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Renal Tissue ◽  
Elongation Factors ◽  
Elongation Factor 2 ◽  
Peptide Elongation ◽  
Elongation Factor 1 ◽  
Trna Binding

Rats received two injections (each 2.6 mg/kg body wt.) of CdCl2, and the kidneys were removed 24 h later. Postmicrosomal supernatant fractions of the homogenized kidneys were used as a source of elongation factors 1 and 2 in assays for [14C]phenylalanyl-tRNA binding to ribosomes and for peptide-bond synthesis. After purification of these preparations by precipitation with (NH4)2SO4 and gel filtration on Sephadex G-200 and G-100, elongation factor 1 activity was significantly increased. A significant increase in the activity of purified elongation factor 2 was also found. The results are discussed in relation to the reported effects of CdCl2 and of HgCl2 on renal tissue.

ADENOSINETRIPHOSPHATASE STUDY DURING RAT LIVER DAMAGE

1952 ◽  
Vol 30 (4) ◽  
pp. 295-301
Author(s):  
Claude Allard ◽  
Antonio Cantero
Keyword(s):  
Cell Division ◽  
Liver Regeneration ◽  
Rat Liver ◽  
Liver Damage ◽  
Liver Tumor ◽  
High Rate ◽  
Supernatant Fraction ◽  
Regenerating Liver ◽  
Albino Rat ◽  
Soluble Part

Adenosinetriphosphatase activity of the adult albino rat liver varies during stimulated growth caused by partial hepatectomy. Effectively the mitochondrion loses 48% of ATP-ase activity during the first day of regeneration and begins to recuperate ATP-ase activity only after the eighth day of regeneration. Most probably the microsomes (small granules) or the soluble part of the cell are the site of ATP-ase activity fluctuation during rat liver regeneration. The nuclei ATP-ase activity is relatively constant during regeneration. A low ATP-ase activity in the mitochondrion and supernatant fraction of the cell corresponds to a high rate of cell division. The ATP-ase activity of the regenerating liver is different from the ATP-ase activity of the liver tumor.

Multiple forms and some properties of aminoacyltransferase I (elongation factor 1) from rat liver

Biochemistry ◽  
1972 ◽  
Vol 11 (22) ◽  
pp. 4187-4194 ◽  
Author(s):  
James F. Collins ◽  
Hong Mo Moon ◽  
Elizabeth S. Maxwell
Keyword(s):  
Rat Liver ◽  
Elongation Factor ◽  
Multiple Forms ◽  
Elongation Factor 1
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