5′-Nucleotidase of chicken liver: A comparison of soluble 5′-nucleotidase activities in chicken and rat liver

Naito, Yoshitsugu; Itoh, Roichi; Tsushima, Kenji

doi:10.1016/0020-711x(74)90114-1

Cited by 19 publications

(5 citation statements)

References 12 publications

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“…We can thus conclude that the bovine cDNA encodes a 5h-nucleotidase\ phosphotransferase. The hydrolysing specific activity we obtained, 83.3 µmol\min per mg of protein, was higher than that reported for other sources, which ranged from a minimum of 1.1, for 5hN purified from Artemia [4], to a maximum of 37 µmol\min per mg for the chicken liver enzyme [22]. Discrepancies between the specific activities can probably be ascribed to the carry-over, during long purification procedures, of inactive protein.…”

Section: Discussioncontrasting

confidence: 68%

Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli

Allegrini

Pesi

Tozzi

et al. 1997

Biochemical Journal

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A cDNA coding for bovine cytosolic IMP/GMP-specific 5'-nucleotidase endowed with phosphotransferase activity was cloned from calf thymus RNA, by 5' and 3' rapid amplification of cDNA ends protocols (5' and 3' RACE). Two products were isolated: a 5' RACE 1.6 kb fragment and a 3' RACE 2.0 kb fragment, with an overlapping region of 505 bp, leading to a total length of approx. 2951 bp. The similarity in the coding region to that of the human 5'-nucleotidase cDNA sequence [Oka, Matsumoto, Hosokawa and Inoue (1994) Biochem. Biophys. Res. Commun. 205, 917-922], indirectly identified as a 5'-nucleotidase, was 94% and the deduced amino acid sequences were 99.5% identical. The bovine cDNA sequence included the sequences codifying for six peptides obtained from 5'-nucleotidase/phosphotransferase purified from calf thymus. Northern blots of human mRNA species from different tissues showed a 3.6 kb mRNA expressed at equal levels in most tissues. The cDNA was cloned into a pET-28c expression vector and the protein obtained after induction had a molecular mass of 61 kDa under SDS/PAGE. It exhibited both 5'-nucleotidase and phosphotransferase activity, as well as immunological and kinetic properties similar to those of the enzyme purified from calf thymus. This is the first time that a fully active recombinant 5'nucleotidase has been described.

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Section: Discussioncontrasting

confidence: 68%

Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli

Allegrini

Pesi

Tozzi

et al. 1997

Biochemical Journal

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“…This is in contrast with rat hepatocytes subjected to anoxia, in which the production of uric acid was not influenced by inhibition of adenosine deaminase (Vincent et al, 1982). The difference may be explained by a more active 5'-nucleotidase (Naito et al, 1974) or by a less active recycling of adenosine in chicken hepatocytes as compared with rat liver cells. The observation that adenosine accumulated in the absence (Figs.…”

Section: Discussioncontrasting

confidence: 56%

“…In contrast, form II of chicken liver AMP deaminase displays hyperbolic kinetics and a lower Km for AMP, is less ATP-dependent, and may be less effective in controlling the degradation of AMP when its concentration is elevated. Another factor in the more rapid catabolism of AMP in isolated chicken hepatocytes may be the above-mentioned several-fold higher activity of the cytosolic 5'-nucleotidase in chicken as compared with rat liver (Naito et al, 1974). The accumulation of inosine, hypoxanthine and xanthine ( Figs.…”

Section: Discussionmentioning

confidence: 99%

Adenine nucleotide metabolism in isolated chicken hepatocytes

Spychała¹,

Berghe²

1987

Biochemical Journal

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The turnover of the adenine nucleotide pool, the pathway of the degradation of AMP and the occurrence of recycling of adenosine were investigated in isolated chicken hepatocytes, in which the adenylates had been labelled by prior incubation with [14C]adenine. Under physiological conditions, 85% of the IMP synthesized by the 'de novo' pathway (approx. 37 nmol/min per g of cells) was catabolized directly via inosine into uric acid, and 14% was converted into adenine nucleotides. The latter were found to turn over at the rate of approx. 5 nmol/min per g of tissue. Inhibition of adenosine deaminase by 1 microM-coformycin had no effect on the formation of labelled uric acid, indicating that the initial degradation of AMP proceeds by way of deamination rather than dephosphorylation. Inhibition of adenosine kinase by 100 microM-5-iodotubercidin resulted in a loss of labelled ATP, demonstrating that adenosine is normally formed from AMP but is recycled. Unexpectedly, 5-iodotubercidin did not decrease the total concentration of ATP, indicating that the loss of adenylates caused by inhibition of adenosine kinase was nearly completely compensated by formation of AMP de novo. Anoxia induced a greatly increased catabolism of the adenine nucleotide pool, which proceeded in part by dephosphorylation of AMP. On reoxygenation, the formation of AMP de novo was increased 8-fold as compared with normoxic conditions. The latter results indicate the existence of adaptive mechanisms in chick liver allowing, when required, channelling of the metabolic flux through the 'de novo' pathway, away from the uricotelic catabolic route, into the synthesis of adenine nucleotides.

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“…This behavior is thought to be due to the activity of 5'nucleotidase and possibly guanase (25). The activity of 5'-nucleotidase in the avian liver is quite high compared to the rat (26). The avian enzyme expresses greatest activity towards IMP and GMP and is believed to participate significantly in the degradation of these nucleotides to uric acid in the uricotelic animal (27,28).…”

Section: Acetone Powder Preparationmentioning

confidence: 93%

Purine Metabolism in High- and Low-Uric Acid Lines of Chickens: Hypoxanthine/Guanine Phosphoribosyltransferase Activities

McFarland

Coon

1983

Experimental Biology and Medicine

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The activity of hypoxanthine/guanine phosphoribosyltransferase (HGPRT) was examined in the livers and kidneys of two genetic lines of chickens selected for different plasma uric acid levels. Previous work demonstrated that the high-uric acid line (HUA) had significantly greater de novo uric acid synthesis rates in kidney tissue compared to the low-uric acid line (LUA). In addition, phosphoribosylpyrophosphate (PRPP) synthetase and xanthine dehydrogenase activities in livers and kidneys were significantly higher in the HUA compared to the LUA line. PRPP pool sizes were also significantly higher in both livers and kidneys of HUA birds. HGPRT activities in livers of HUA birds were significantly (P -c 0.05) greater than in LUA birds. The mean value of liver HGPRT was 7.36 f 0.25 pmole inosine-5'-monophosphate (IMP) and 6.05 f 0.27 pmole IMP produced/pg protein/hr, respectively, for the HUA and LUA lines. There were no significant differences (P > 0.05) in kidney HGPRT activities between the two groups. The mean value of kidney HGPRT was 52.87 f 1.62 pmole IMP and 50.72 f 1.62 pmole IMP produced/pg protein/hr, respectively, for the HUA and LUA line. Elevated liver HGPRT may serve to enhance the regeneration of PRPP in the HUA liver. Elevated liver PRPP synthetase and PRPP pool size suggest an increased flux through the de novo purine biosynthetic pathway in HUA birds. The resulting additional pyrophosphate from the glutamine PRPP amidotransferase reaction would stimulate recovery of PRPP and spare the system from a substantial loss of energy.

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5′-Nucleotidase of chicken liver: A comparison of soluble 5′-nucleotidase activities in chicken and rat liver

Cited by 19 publications

References 12 publications

Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli

Bovine cytosolic IMP/GMP-specific 5′-nucleotidase: cloning and expression of active enzyme in Escherichia coli

Adenine nucleotide metabolism in isolated chicken hepatocytes

Purine Metabolism in High- and Low-Uric Acid Lines of Chickens: Hypoxanthine/Guanine Phosphoribosyltransferase Activities

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