scholarly journals Activity of nicotinamide–adenine dinucleotide pyrophosphorylase in liver nuclei. Effects of partial hepatectomy, hepatotoxins and dietary changes

1968 ◽  
Vol 108 (1) ◽  
pp. 89-93
Author(s):  
F. Stirpe ◽  
E. Della Corte
Keyword(s):  
Enzyme Activity ◽  
Partial Hepatectomy ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Mouse Liver ◽  
Actinomycin D ◽  
Newborn Rats ◽  
Dietary Changes ◽  
Liver Nuclei ◽  
Protein Free Diet

1. The activity of NAD pyrophosphorylase is lower in nuclei isolated from regenerating rat liver than in normal nuclei, and this is due to leakage of the enzyme from the nuclei during the isolation. 2. The NAD pyrophosphorylase activity is lower in liver nuclei from newborn rats, and from rats on a protein-free diet, but no leakage occurs in these cases. 3. Poisoning with α-amanitin brings about a transient enhancement of NAD pyrophosphorylase activity in mouse liver nuclei. 4. No changes of enzyme activity were observed after 72hr. starvation, administration of actinomycin D or infection with MHV3 virus.

scholarly journals The fractionation of nuclei from mammalian cells by zonal centrifugation

1968 ◽  
Vol 109 (1) ◽  
pp. 127-135 ◽  
Author(s):  
I R Johnston ◽  
A P Mathias ◽  
F. Pennington ◽  
D. Ridge
Keyword(s):  
Rat Liver ◽  
Mammalian Cells ◽  
Mouse Liver ◽  
The Other ◽  
Slow Speed ◽  
Adult Rats ◽  
Sucrose Solutions ◽  
Liver Nuclei ◽  
Effect Of Age ◽  
Zonal Rotor

1. Purified liver nuclei from adult rats separate into two main zones when centrifuged in the slow-speed zonal rotor. One zone contains diploid nuclei, the other tetraploid. 2. The effect of age on the pattern of rat liver ploidy was examined. Tetraploid nuclei are virtually absent from young animals. They increase in proportion steadily with age. Partial hepatectomy disturbs the pattern of ploidy. 3. The zonal centrifuge permits the separation of diploid, tetraploid, octaploid and hexadecaploid nuclei from mouse liver. 4. Rat liver nuclei are isopycnic with sucrose solutions of density 1·35 at 5°.

scholarly journals Biphasic effect of acute ethanol administration on rat liver tyrosine-2-oxoglutarate aminotransferase activity

1980 ◽  
Vol 186 (3) ◽  
pp. 755-761 ◽  
Author(s):  
A A B Badawy ◽  
B M Snape ◽  
M Evans
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Actinomycin D ◽  
Tyrosine Aminotransferase ◽  
Ethanol Metabolism ◽  
Ethanol Administration ◽  
Aminotransferase Activity ◽  
Biphasic Effect ◽  
Initial Decrease ◽  
Acute Ethanol

1. Acute ethanol administration causes a biphasic change in rat liver tyrosine aminotransferase activity. 2. The initial decrease is significant with a 200 mg/kg dose of ethanol, is prevented by adrenoceptor-blocking agnets and by reserpine, but not by inhibitors of ethanol metabolism, and exhibits many of the characteristics of the inhibition caused by noradrenaline. 3. The subsequent enhancement of the enzyme activity by ethanol is not associated with stabilization of the enzyme, but is sensitive to actinomycin D and cycloheximide. 4. It is suggested that the initial decrease in aminotransferase activity is caused by the release of catecholamines, whereas the subsequent enhancement may be related to the release of glucocorticoids.

scholarly journals Intracellular enzymes of collagen biosynthesis in rat liver as a function of age and in hepatic injury induced by dimethylnitrosamine. Purification of rat prolyl hydroxylase and comparison of changes in prolyl hydroxylase activity with changes in immunoreactive prolyl hydroxylase

1976 ◽  
Vol 158 (2) ◽  
pp. 369-376 ◽  
Author(s):  
J Risteli ◽  
L Tuderman ◽  
K I Kivirikko
Keyword(s):  
Enzyme Activity ◽  
Rat Liver ◽  
Hepatic Injury ◽  
Specific Activity ◽  
Prolyl Hydroxylase ◽  
Newborn Rats ◽  
Hydroxylase Activity ◽  
Immunoreactive Protein ◽  
Molecular Weights ◽  
Polypeptide Chains

Prolyl hydroxylase was purified from newborn rats by affinity chromatography using poly(L-proline), and antiserum to the enzyme was prepared in rabbits. The rat prolyl hydroxylase was similar to the chick and human enzymes with respect to specific activity, molecular weight and molecular weights of the polypeptide chains. The activity of prolyl hydroxylase and the content of immunoreactive enzyme were measured in rat liver as a function of age in experimental hepatic injury. Active prolyl hydroxylase comprised about 13.2% of the total immunoreactive protein in the liver of newborn rats and the value decreased to about 3.6% at the age of 420 days. This decrease was due to a decrease in the enzyme activity, whereas only minor changes were found in the content of the immunoreactive protein. In hepatic injury, a significant increase was found in the ratio of active enzyme to total immunoreactive protein, owing to an increase in the enzyme activity. The data indicate that prolyl hydroxylase activity in rat liver is controlled in part by a mechanism which does not involve changes in the content of the total immunoreactive protein.

scholarly journals The metabolism of nicotinamide-adenine dinucleotide in various classes of rat liver nuclei

1969 ◽  
Vol 115 (5) ◽  
pp. 56P-56P
Author(s):  
M E Haines ◽  
I R Johnston ◽  
A P Mathias ◽  
D Ridge
Keyword(s):  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

scholarly journals The synthesis of nicotinamide–adenine dinucleotide and poly(adenosine diphosphate ribose) in various classes of rat liver nuclei

1969 ◽  
Vol 115 (5) ◽  
pp. 881-887 ◽  
Author(s):  
M E Haines ◽  
I R Johnston ◽  
A P Mathias ◽  
D. Ridge
Keyword(s):  
Dna Synthesis ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Adenosine Diphosphate ◽  
Nicotinamide Adenine ◽  
Nad Metabolism ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Specific Activities

1. The activities of NMN adenylyltransferase and an enzyme that synthesizes poly (ADP-ribose) from NAD were investigated in the various classes of rat liver nuclei fractionated by zonal centrifugation. 2. The highest specific activities of these two nuclear enzymes occur in different classes of nuclei. In very young and in mature rats it was shown that a correlation exists between DNA synthesis and NMN adenylyltransferase activity, but in rats of intermediate age this correlation is less evident. The highest activities of the enzyme that catalyses formation of poly (ADP-ribose) are in the nuclei involved in the synthesis of RNA. 3. The significance of these results in relation to NAD metabolism is discussed.

scholarly journals A NUCLEAR MEMBRANE CHANGE AFTER PARTIAL HEPATECTOMY

1964 ◽  
Vol 23 (3) ◽  
pp. 511-518 ◽  
Author(s):  
Susumu Kishimoto ◽  
Irving Lieberman
Keyword(s):  
Electrophoretic Mobility ◽  
Partial Hepatectomy ◽  
Nuclear Membrane ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
Rate Increase ◽  
Fold Increase ◽  
Liver Nuclei ◽  
The Difference ◽  
Membrane Change

Partial hepatectomy (67 per cent extirpation) of the rat leads to a change in the membrane of liver nuclei (purified with citric acid) detectable as an increase in electrophoretic mobility. No change is detectable 2 hours after the operation, but between 2 and 6 hours about a 1.4-fold increase in mobility occurs after which the mobility becomes constant at the elevated level. Removal of only 10 per cent of the liver causes no detectable change in 6 hours. Bilateral adrenalectomy immediately before partial hepatectomy does not affect the development of the nuclear change. Actinomycin D and p-fluorophenylalanine, but not noradrenalin, ionizing radiation, or EDTA, suppress the increase in electrophoretic mobility. The level of actinomycin D required to block the nuclear membrane change is 6 times greater than that necessary to prevent the rate increase in hepatic RNA metabolism that follows removal of part of the liver. This discrepancy and the difference in the response to noradrenalin indicate that, at least initially, the nuclear membrane change and the change in the rate of RNA synthesis are independent processes. The inability of EDTA to block the nuclear membrane change shows that the Zn++ requirement for DNA replication is not related to the events that lead to the alteration in the electrokinetic properties of liver nuclei.

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