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)

The soluble fraction of uterine tissue was found to contain a factor which is a potent activator of various cyclic nucleotide phosphodiesterases (with the exception of the retinal photoreceptor cell enzyme). The protein origin of this factor was established, using proteolysis, precipitation with trichloroacetic acid. The activator was purified by gel filtration on Sephadex G-25 and Biogel P-4 as well as by a highly effective liquid chromatography. The activator was shown to be a peptide with Mr = 1150 Da. The peptide was thermostable and stable within a broad range of pH. Besides phosphodiesterases, the peptide activated 5'-nucleotidase and Mg2+-ATPase of photoreceptor membranes.
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PMID:[Detection of peptide, an activator of cyclic nucleotide phosphodiesterases, in uterine tissue]. 282 12

A new 5'-nucleotidase inhibitor named nucleoticidin was produced by Pseudomonas sp. YM-3229G. It was isolated from a fermentation broth by trichloroacetic acid extraction, ethanol precipitation and Dowex 1 and DEAE-52 column chromatography. It inhibited 5'-nucleotidase activity of snake venom and rat liver membrane. It also showed antitumor activity against solid type Sarcoma 180.
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PMID:A new 5'-nucleotidase inhibitor, nucleoticidin. I. Taxonomy, fermentation, isolation and biological properties. 298 70

Prolactin proteolysis by rat pituitary homogenates was assayed by measuring the release of trichloroacetic acid-soluble peptides from 125I-labelled rat prolactin. There was a distinct optimum at pH 4.3, with only trace amounts of activity at neutral and alkaline pH. Rat pituitary homogenates were subjected to analytical subcellular fractionation by sucrose density gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their respective marker enzymes, including: cytosol (lactate dehydrogenase); plasma membrane (5'-nucleotidase); lysosomes (N-acetyl-beta-glucosaminidase, beta-glucuronidase); mitochondria (particulate malate dehydrogenase); endoplasmic reticulum (neutral alpha-glucosidase); prolactin granules (radioimmunoassayable prolactin). Acid prolactin protease had a similar distribution to the lysosomal marker enzymes. A localisation of the activity to lysosomes was confirmed by subcellular fractionation experiments in which the lysosomes were selectively disrupted with low concentrations of the membrane perturbant, digitonin. Experiments with specific inhibitors of the lysosomal cathepsins indicate that both cathepsins B and D are implicated in pituitary prolactin proteolysis.
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PMID:Analytical subcellular fractionation of rat pituitary homogenates, with special reference to prolactin proteolysis by lysosomes. 729 6

The development of satisfactory cell culture models for the study of parathyroid hormone (PTH)-induced inhibition of Pi transport has proven difficult. Using subcellular fractionation techniques we investigated the response of primary cultures of rat proximal tubular cells to PTH-(1-34). Specific binding of 125I-bPTH-(1-34) occurred at 2 degrees C. After 5 min of rewarming, trypsin-releasable radioactivity decreased from 90 to 50%, indicating internalization of the ligand. Cell disruption, followed by density centrifugation with 17% Percoll either directly after binding at 2 degrees C or post-rewarming for 20 min, showed a shift of 125I label from the plasma membrane (5'-nucleotidase) to lysosomal fractions (beta-D-glucosaminidase), confirming the sequential occurrence of cell surface binding, internalization and transport to lysosomes of 125I-bPTH-(1-34). Reculture at 37 degrees C revealed steady accumulation of trichloroacetic acid-soluble radioactivity in the medium, indicating degradation of 125I-bPTH-(1-34). Phosphate transport in the absence of sodium was minimal. Incubation of the cells with bPTH-(1-34) resulted in up to 50% inhibition of sodium-dependent phosphate transport. Prior phosphate depletion abrogated the response to PTH.
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PMID:Parathyroid hormone transport effects and hormonal processing in primary cultured rat proximal tubular cells. 834 17