Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.5 (5'-nucleotidase)
3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Some physico-chemical properties, specificity and the character of action of rat liver nuclear ribonuclease are studied. The enzyme maximal activity was observed at pH 7.5--8.0, ionic strength 0.02--0.3, Mg2+ being necessary. Nuclease is an oligomer, having molecular weight is 160000--180000 daltons and containing separate associates. Purified enzyme is free of contaminating activities (polynucleotidephosphorylase, DNAse; 5'-nucleotidase, and alkaline phosphatases). It is shown to hydrolyse polyA and RNA for endonuclease type, degradation products being oligonucleotides terminating with 5'-phosphate and 3'-hydroxyl groups. RNAse hydrolyses all phosphodiester bonds in polynucleotides, developing no specificity to the nature of bases. Relative hydrolysis rate for different substrates decreased as follows: polyA greater than yeast RNA greater than polyC greater than polyU greater than 28S rRNA greater than greater than 18S rRNA greater than polyA-polyU. The enzyme may be classified as ribonucleate-5'-nucleotidehydrolase (EC 3.1.4.9.).
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PMID:[Nuclear ribonucleases and post-transcriptional changes of RNA. Specificity and other properties of rat liver nuclear endonuclease]. 1 31

We have perfused isolated rat livers with hypocalcemic (4.4 mg 100 ml) Krebs-Ringer bicarbonate albumin buffer. After 15 min of perfusion, a substance appeared in the perfusate which decreased rat renal adenylate cyclase activation by parathyroid hormone (PTH). The material in the perfusate was purified greater than 50,000-fold by Bio-Gel P-10 chromatography. The purified antagonist decreased the activation of rat renal cortical adenylate cyclase by PTH, glucagon, and epinephrine 75 to 100%. Concentration response curves for each of the hormones indicated a noncompetitive interaction of the inhibitor with the hormone. The inhibition was not species-specific, as the activation of the parathyroid hormone-responsive adenylate cyclase in cat renal cortex was also abolished by the inhibitor from the perfused rat liver. The inhibitor is a peptide, Mr equal to similar to 1000, which is heat-stable, acid-stable, alkai-labile, and is destroyed by trypsin, leucine aminopeptidase, and elastase. It is not destroyed by phosphodiesterase, 5'-nucleotidase, alkaline phosphatase, neuraminidase, RNase, or phospholipase A. The inhibitor is not produced by isolated rat livers perfused with normocalcemic perfusion media. It is unclear whether the peptide is synthesized by the liver or whether it is a breakdown product of a larger peptide or protein in the liver. This is the first reported peptide inhibitor of adenylate cyclase.
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PMID:Isolation of a unique peptide inhibitor of hormone-responsive adenylate cyclase. 16 24

Dialysis, gel-chromatography on Sephadex G-75 (superfine) and chromatography on sulphoethylcellulose give high yield (68 per cent) of 162-fold purified ribonuclease from cobra venom. In ion-exchange chromatography, ribonuclease is eluted in two fractions. The fraction with the highest specific activity has a molecular weight of 15900 and is homogeneous in 15 per cent polyacrilamide gel electrophoresis at pH 8.9. Electrophoresis at pH 4.3 reveals a minor fast component of this fraction which also exhibits a ribonuclease activity. Sulphoethylcellulose chromatography fairly separates cobra venom phosphodiesterase and 5'-nucleotidase eluted as a single fraction in gel chromatography.
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PMID:[Isolation of highly purified ribonuclease from cobra (Naja oxiana) venom]. 17 25

Pseudomonas aeruginosa (ATCC 9027) releases four periplasm-located enzymes, i.e., ribonuclease (EC 3.1.4.22; EC 3.1.4.23), alkaline phosphatase (EC 3.1.3.1), cyclic-2', 3'-phosphodiesterase (EC 3.1.4.d), and 5'-nucleotidase (EC 3.1.3.5) into the medium during growth. Ribonuclease and alkaline phosphatase are classed as enzymes which are readily extracted by osmotic shock and spheroplast formation whereas cyclic-2',3'-phosphodiesterase and 5'-nucleotidase are classed as enzymes which are not readily extracted by these procedures. In view of the relative ease of extraction of the former enzymes it is suggested that the lattter enzymes, cyclic-2',3'-phosphodiesterase and 5'-nucleotidase, are bound and located in the periplasm in a manner different to ribonuclease and alkaline phosphatase.
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PMID:The release and characterization of some periplasm-located enzymes of Pseudomona aeruginosa. 18 95

The activity of 5'-nucleotidase (EC 1.3.5), cyclic nucleotide phosphodiesterase (EC 2.1.4.17), non-specific phosphodiesterase (EC 3.1.4.1) and ribonuclease (EC 1.7.7.16)has been investigated in the seminal plasma of whole semen and in the secretions of the seminal vesicle, prostate and epididymis of the bull, boar, ram, stallion, jackass, rabbit and man. Bull seminal plasma showed the highest activity for 5'-nucleotidase, cyclic nucleotide phosphodiesterase and ribonuclease; in contrast, stallion and jackass semen were very poor in these enzymes. Ram, rabbit and boar seminal plasma showed intermediate levels for all enzymes studied. In the bull and ram, nucleolytic enzymes were found to be secreted by the seminal vesicles but in the boar, rabbit and stallion they originate mostly from the epididymis. In human seminal plasma all of the enzymes studied exhibited activity but the levels were generally lower than those recorded for the other species.
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PMID:The activity of some nucleolytic enzymes in semen and in the secretion of the male reproductive tract. 19 15

A comparative study of glucose-6-phosphatase, alcaline RNase, ATPase, inosine diphosphatase and 5'-nucleotidase activities in isolated rat liver and hepatoma-27 nuclei and nuclear envelopes was performed. The tumor nuclear membranes were shown to be free from G-6-Pase activity in contrast to the liver nuclear membranes. The nuclear RNase activity was strongly inhibited in the hepatoma and could be unmasked in the presence of 3-10(-4) M pCMB. Hepatoma nuclear and nuclear envelopes ATP-ase activity was found to be moderately decreased as compared to those of the normal tissue. The values of inosine diphosphatase activity in hepatoma were similar to those in liver. The role of the nuclear envelope in nuclear-cytoplasmic interactions as well as nuclear location of G-6-Pase are discussed.
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PMID:[Various enzymes of isolated nuclear membranes and cell nuclei of the liver and hepatoma 27 of rats]. 19 29

The enzymes from the venom of Heterometrus scaber, the indole compounds present and the toxic protein of the venom have been studied. The venom contains acid phosphatase, ribonuclease, 5'-nucleotidase, hyaluronidase, acetylcholine esterase and phospholipase. A. The indole compounds present in the venom have been identified as 5-hydroxytryptophan, tryptophan, serotonin and tryptamine, along with two unidentified indole compounds. The venom produces hyperglycaemia in sublethal doses and this has been found to be due to increased adrenaline secretion. The toxic protein of the venom has been obtained in a pure form by (NH4)2SO4 fractionation, followed by fractional precipitation with acetone and chromatography over DEAE-Sephadex. The toxic fraction has been found to be homogeneous on acrylamide gel electrophoresis. It is a glycoprotein (molecular weight 15 000) containing 1.74% glucosamine, 0.87% galactosamine, 0.313% sialic acid, 3.25% fucose and 0.45% of an unidentified neutral sugar. It did not show any enzyme activities, haemolytic activity or inhibition of succinate dehydrogenase activity but it produced hyperglycaemia in sublethal doses. The toxic level (intravenous administration in rats) was found to be 0.72 mg/kg body weight.
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PMID:Investigations on the venom of the South Indian scorpion Heterometrus scaber. 111 82

D-Galactosamine (800 mg/kg, intraperitoneally) caused significant decrease in the activities of 5'-nucleotidase, glucose-6-phosphatase and cytochrome P450 and increase in activities of gamma-glutamyl transpeptidase, succinate dehydrogenase, acid phosphatase and acid ribonuclease in liver after 24 hr. The levels of RNA, protein and glycogen decreased while total lipids, phospholipids, cholesterol and lipid peroxides increased. It also increased the serum levels of transaminases, alkaline phosphatase and bilirubin while protein concentration decreased significantly. Oral administration of Picroliv (12 mg/kg/day for 7 days), a standardised iridoid glycoside fraction of Picrorhiza kurroa, significantly prevented the biochemical changes in liver and serum of galactosamine-toxicated rats. Kutkoside (12 mg/kg/day for 7 days) also protected against changes in most of the hepatic and serum constituents studied. Another iridoid glycoside from Picroliv, Picroside I, at the same dose level could only prevent toxicant-induced changes in acid phosphatase, phospholipids and lipid peroxides in liver and alkaline phosphatase in serum. Mixture of Picroside I and Kutkoside in the ratio of 1:1.5 at 12 mg/kg dose elicited lesser response than Picroliv.
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PMID:Picroliv and its components kutkoside and picroside I protect liver against galactosamine-induced damage in rats. 133 78

The efficacy of Picroliv, a standardized iridoid glycoside fraction of Picrorhiza kurroa, was studied against the Amanita phalloides-induced biochemical changes in rat liver. A phalloides (50 mg.kg-1) caused significant increases in the activities of hepatic 5'-nucleotidase, gamma-glutamyl transpeptidase, acid ribonuclease, and succinate dehydrogenase, but a decrease in glucose-6-phosphatase. The level of cytochrome P-450 in microsomal fraction and content of glycogen in liver showed significant depletions. Picroliv (25 mg.kg-1.d-1 x 10 d) provided significant restorations of all the biochemical changes poisoned by A phalloides except cytochrome P-450 and glycogen. These results demonstrated the protective effect of Picroliv against A phalloides-induced hepatotoxicity in rats.
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PMID:Effects of picroliv, the active principle of Picrorhiza kurroa, on biochemical changes in rat liver poisoned by Amanita phalloides. 135 30

Monocrotaline, a pyrrolizidine alkaloid, caused changes in most of the biochemical parameters in rats 12 days after a single dose of 120 mg/kg. These included significantly increased activities of hepatic succinate dehydrogenase, acid ribonuclease, acid phosphatase, gammaglutamyl transpeptidase and 5'-nucleotidase and decreased in the activities of glucose-6-phosphatase and cytochrome P450. The levels of DNA, RNA and glycogen in liver and albumin and protein in serum decreased while serum bilirubin increased. The histopathological changes in liver were characterized by diffused hepatocyte alterations in the form of ballooning, granular cytoplasm, indistinct cell outlines, nuclear changes, focal necrosis, and vascular damage. When picroliv, a standardized iridoid glycoside fraction of Picrorhiza kurroa, was administered orally in a dose of 25 mg/kg simultaneously with monocrotaline, alterations in most of the biochemical parameters along with the histopathological changes in liver caused by monocrotaline were prevented.
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PMID:Picroliv protects against monocrotaline-induced hepatic damage in rats. 190 81


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