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Soluble inorganic pyrophosphatase fromSchizophyllum commune
Folia Microbiologica, 1983The specific activity of inorganic pyrophosphatase (EC 3.6.1.1) fromSchizophyllum commune correlated with the growth pattern so that actively dividing cells contained the highest enzyme activities. Continuous illumination which induce a certain series of morphogenetic events in the colony, exhibited no specific effects on the enzyme activity. There was
R. Lahti, M. Raudaskoski
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Characterization of a soluble inorganic pyrophosphatase from chicken liver
International Journal of Biochemistry, 1975Abstract 1. 1. Characteristics of the inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1) activity in the dialyzed cytosol fraction of homogenates from livers of 4-daychicks ( Gallus gallus ) have been determined. 2. 2. This soluble enzyme, which exhibits maximum activity between pH 7.5 and 8.0, is relatively specific for ...
Patsy Wang, Cornelius F. Strittmatter
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Purification and Properties of a Soluble Inorganic Pyrophosphatase fromRhodopseudomonas palustris
Biological Chemistry Hoppe-Seyler, 1986A soluble inorganic pyrophosphatase from photolithoautotrophically grown Rhodopseudomonas palustris was purified to a state of apparent homogeneity applying high resolving liquid chromatography steps. Values of 65 500 and 64 500 were calculated for the relative molecular mass under non-dissociating conditions employing gel filtration and high ...
H M, Schwarm, H, Vigenschow, K, Knobloch
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Characterization of two soluble inorganic pyrophosphatases from Arabidopsis thaliana
Plant Science, 2007Abstract Inorganic pyrophosphatases (siPPiase) catalyze the irreversible hydrolysis of pyrophosphate and their function is known to be essential to all living organisms. In this work, the cDNAs coding for two Arabidopsis thaliana siPPiase were obtained from the TAIR initiative and cloned in an expression vector as fusions with gluthathione-S ...
Ernesto Navarro-De la Sancha +5 more
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Plant Molecular Biology, 1999
Using polyclonal antibodies raised against a previously cloned potato Mg2+-dependent soluble inorganic pyrophosphatase (ppa1 gene) [8], a second gene, called ppa2, could be isolated. A single locus homologous to ppa2 was mapped on potato chromosomes, unlinked to the two loci identified for ppa1.
J A, Rojas-Beltrán +6 more
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Using polyclonal antibodies raised against a previously cloned potato Mg2+-dependent soluble inorganic pyrophosphatase (ppa1 gene) [8], a second gene, called ppa2, could be isolated. A single locus homologous to ppa2 was mapped on potato chromosomes, unlinked to the two loci identified for ppa1.
J A, Rojas-Beltrán +6 more
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Plant Science, 2012
Phosphorus is an essential element for all living cells, but its availability is often limiting in the soil. Plants have adapted to such limitation and respond to phosphorus deficiency. The soluble inorganic pyrophosphatases (PPase; EC 3.6.1.1) recycle the pyrophosphate produced by many biosynthetic reactions, and may play a role in the plant ...
Eric E, Hernández-Domíguez +2 more
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Phosphorus is an essential element for all living cells, but its availability is often limiting in the soil. Plants have adapted to such limitation and respond to phosphorus deficiency. The soluble inorganic pyrophosphatases (PPase; EC 3.6.1.1) recycle the pyrophosphate produced by many biosynthetic reactions, and may play a role in the plant ...
Eric E, Hernández-Domíguez +2 more
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Insect Molecular Biology, 2017
Abstract Polyphosphates have been found in all cell types examined to date and play diverse roles depending on the cell type. In eukaryotic organisms, polyphosphates have been investigated mainly in mammalian cells, and only a few studies have addressed arthropods.
C. S. Cruz +10 more
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Abstract Polyphosphates have been found in all cell types examined to date and play diverse roles depending on the cell type. In eukaryotic organisms, polyphosphates have been investigated mainly in mammalian cells, and only a few studies have addressed arthropods.
C. S. Cruz +10 more
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New Phytologist, 2018
Summary Apple exhibits S‐RNase‐based self‐incompatibility (SI), in which S‐RNase plays a central role in rejecting self‐pollen. It has been proposed that the arrest of pollen growth in SI of Solanaceae plants is a consequence of the degradation of pollen rRNA by S‐RNase; however, the underlying mechanism in Rosaceae is still unclear.
Wei, Li +9 more
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Summary Apple exhibits S‐RNase‐based self‐incompatibility (SI), in which S‐RNase plays a central role in rejecting self‐pollen. It has been proposed that the arrest of pollen growth in SI of Solanaceae plants is a consequence of the degradation of pollen rRNA by S‐RNase; however, the underlying mechanism in Rosaceae is still unclear.
Wei, Li +9 more
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1998
Inorganic pyrophosphatases (sPPase; pyrophosphate phosphohydrolase, EC 3.6.1.1) are essential enzymes found in the cytosol and cellular organelles that drive anabolism through the hydrolysis of the energy-nch pyrophosphate (PPi) produced in the synthesis of biological polymers, making these processes thermodinamically irreversible.
R. Gómez +3 more
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Inorganic pyrophosphatases (sPPase; pyrophosphate phosphohydrolase, EC 3.6.1.1) are essential enzymes found in the cytosol and cellular organelles that drive anabolism through the hydrolysis of the energy-nch pyrophosphate (PPi) produced in the synthesis of biological polymers, making these processes thermodinamically irreversible.
R. Gómez +3 more
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Biokhimiia (Moscow, Russia), 1982
Data from sedimentation analysis suggest that modification of about 40% of free amino groups of inorganic pyrophosphatase by maleic anhydride, pH 10.5, results in a loss of the enzyme ability to form dimers at neutral values of pH. The specific activity of monomeric pyrophosphatase is 50-80% of that of the dimeric form.
V N, Kasho +3 more
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Data from sedimentation analysis suggest that modification of about 40% of free amino groups of inorganic pyrophosphatase by maleic anhydride, pH 10.5, results in a loss of the enzyme ability to form dimers at neutral values of pH. The specific activity of monomeric pyrophosphatase is 50-80% of that of the dimeric form.
V N, Kasho +3 more
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