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Nucleotide Pyrophosphatases/Phosphodiesterases on the Move

Critical Reviews in Biochemistry and Molecular Biology, 2000
Nucleotide pyrophosphatases/phosphodiesterases (NPPs) release nucleoside 5'-monophosphates from nucleotides and their derivatives. They exist both as membrane proteins, with an extracellular active site, and as soluble proteins in body fluids. The only well-characterized NPPs are the mammalian ecto-enzymes NPP1 (PC-1), NPP2 (autotaxin) and NPP3 (B10 ...
Hugo Ceulemans   +2 more
exaly   +3 more sources

Inorganic Pyrophosphatases: Study of Interest [PDF]

open access: yesAdvances in Bioscience and Biotechnology (Print), 2017
Inorganic pyrophosphatases are enzymes that catalyze the hydrolysis of inorganic pyrophosphate to orthophosphate. These enzymes are divided into two groups: the soluble pyrophosphatases and the membrane pyrophosphatases.
Elkhalfi, Bouchra   +4 more
exaly   +3 more sources

Pyrophosphatases of bone

Experientia, 1958
Si e studiata l'attivita pirofosfatasica, de terminandone il pH ottimale, in 9 frazioni scheletriche istologicamente uniformi: cartilagine articolare e cartilagine di coniugazione, osso spongioso epi e metafisario, osso compatto, midollo diafisario, midollo dell'osso spongioso epifisario e dell'osso spongioso metafisario, periostio.
P, CERLETTI, P L, IPATA, G, TANCREDI
openaire   +2 more sources

The magnesium activation of pyrophosphatase

Archives of Biochemistry and Biophysics, 1955
Abstract The activity of rat brain pyrophosphatase at various concentrations of added Mg++ and inorganic pyrophosphate has been measured. In confirmation and extension of previous results the data show a pronounced inhibition of the enzyme action by pyrophosphate and a weaker inhibition by excess magnesium pyrophosphate.
E A, ROBBINS, M P, STULBERG, P D, BOYER
openaire   +2 more sources

Tobacco nucleotide pyrophosphatases

Archives of Biochemistry and Biophysics, 1960
Abstract The intracellular distribution of tobacco root nucleotide pyrophosphatase activity has been investigated. These and related studies have led to the observation that the splitting of ATP and DPN by tobacco preparations is catalyzed by different enzyme systems.
R A, CLAYTON, L M, HANSELMAN
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Histochemical Demonstration of Pyrophosphatase

Stain Technology, 1956
Fresh tissue slices were fixed in 5% formalin containing 0.9% NaCl for 10-20 min and frozen sections therefrom floated for 3 hr at 37°C on an incubating mixture made as follows. Sodium pyrophosphate (Na4P2O7-12H2O), 1.088 gm was dissolved in 20-30 ml of distilled water and to this was added ferric chloride (FeCl3-6H2O), 0.61 gm dissolved in 10-15 ml of
Y, KURATA, S, MAEDA
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Chloroplast inorganic pyrophosphatase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1970
Abstract An alkaline, Mg2+-dependent inorganic pyrophosphatase has been isolated from previously isolated spinach chloroplast. The activity of the enzyme was increased 100-fold, with a 42% yield, upon purification from the total soluble chloroplast enzymes. The pH optimum for the enzyme shifts from 9.0 at 5 mM Mg2+ to 7.0 at 40 mM Mg2+. The substrate
A M, el-Badry, J A, Bassham
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Properties of firefly pyrophosphatase

Archives of Biochemistry and Biophysics, 1951
Abstract 1. 1. An enzyme which hydrolyzes inorganic pyrophosphate to orthophosphate has been partially purified from extracts of firefly lanterns. 2. 2. Magnesium ion is essential for enzyme activity; Mn, Zn, Ca, and Be ions are completely inactive. Magnesium ion, at a concentration of 0.00045 M gives 50% of maximum activity. 3. 3.
W D, McELROY, J, COULOMBRE, R, HAYS
openaire   +2 more sources

Cytoplasmic Inorganic Pyrophosphatase

1999
Pyrophosphate (PPi) is the smallest member of the polyphosphate family and is formed by two phosphate (Pi) residues linked by a phosphoanhydride bond. A specific enzyme hydrolyzing PPi to Pi was discovered in animal tissues in 1928 (Kay) and later in a great many other organisms and cell types, in virtually all in which it has been sought.
A A, Baykov   +3 more
openaire   +2 more sources

Phosphatase and pyrophosphatase activities of Aspergilli

Archives of Biochemistry and Biophysics, 1955
Abstract Phosphatase and pyrophosphatase of amylase-elaborating Aspergillus niger (submerged growth) and Aspergillus oryzae (surface culture) have a pH optimum of 4.8, no activity being observable at alkaline pH range. With increase in amylase production in a medium like corn steep liquor or sprouted mung bean extract, there is a corresponding ...
M A, PATHAK, A, SREENIVASAN
openaire   +2 more sources

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