Results 131 to 140 of about 994 (158)
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[Purification and characteristics of Saccharomyces cerevisiae cytosol polyphosphatase].
Biokhimiia (Moscow, Russia), 1997The polyphosphatase with specific activity of 283 units/mg was purified 3450-fold to homogeneity with 3.8% yield from cytosol of Saccharomyces cerevisiae yeast. Polyphosphatase is monomeric 40 kD protein. The enzyme hydrolyzes polyphosphates of various chain length including tripolyphosphate but ATP, pyrophosphate, and p-nitrophenyl phosphate are not ...
N A, Andreeva +2 more
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[Characteristics of polyphosphatase activity of vacuoles in Saccharomyces cerevisiae cells].
Biokhimiia (Moscow, Russia), 1993Vacuoles of the Saccharomyces cerevisiae yeast possess a polyphosphatase activity which differs from other known vacuolar phosphohydrolase activities by pH-optimum, sensitivity towards inhibitors and distribution between the tonoplast and vacuolar sap. The polyphosphatase activity is inhibited by EDTA, molybdate, ortho-vanadate and fluoride. Nearly 77%
N A, Andreeva +3 more
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Biochemistry (Moscow), 2015
The effects of overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) having endopolyphosphatase activity on inorganic polyphosphate metabolism in Saccharomyces cerevisiae were studied. The endopolyphosphatase activity in the transformed strain significantly increased compared to the parent strain.
L V, Trilisenko +4 more
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The effects of overexpression of yeast diphosphoinositol polyphosphate phosphohydrolase (DDP1) having endopolyphosphatase activity on inorganic polyphosphate metabolism in Saccharomyces cerevisiae were studied. The endopolyphosphatase activity in the transformed strain significantly increased compared to the parent strain.
L V, Trilisenko +4 more
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[Characteristics of Saccharomyces cerevisiae nuclear polyphosphatase activity].
Biokhimiia (Moscow, Russia), 1996Saccharomyces cerevisiae nuclei possess a polyphosphatase activity which is insensitive to a number of inhibitors of ATPase and pyrophosphatase (PPase) activities of the same organelle. Heparin, an effective inhibitor of the nuclear polyphosphatase activity, does not alter either the ATPase and PPase activity.
L P, Lichko +2 more
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2009
Mc 2009. Microscopy Conference, Graz, Austria. 30 August - 4 September 2009. First Joint Meeting Of Dreiländertagung And Multinational Congress On Microscopy.
MacLellan, Kirsty +5 more
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Mc 2009. Microscopy Conference, Graz, Austria. 30 August - 4 September 2009. First Joint Meeting Of Dreiländertagung And Multinational Congress On Microscopy.
MacLellan, Kirsty +5 more
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Plant Physiology and Biochemistry
Polyphosphates (poly-P), consisting of two or more phosphate residues, are not directly available to plants and must first be hydrolyzed to orthophosphate (ortho-P). Although microbial polyphosphatase activity is well established, there is currently no evidence for extracellular poly-P-hydrolyzing enzymes produced by plants in the rhizosphere.
Natalie Toren, Ran Erel
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Polyphosphates (poly-P), consisting of two or more phosphate residues, are not directly available to plants and must first be hydrolyzed to orthophosphate (ortho-P). Although microbial polyphosphatase activity is well established, there is currently no evidence for extracellular poly-P-hydrolyzing enzymes produced by plants in the rhizosphere.
Natalie Toren, Ran Erel
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[Detection of polyphosphatase activity in isolated Saccharomyces cerevisiae nuclei].
Biokhimiia (Moscow, Russia), 1996Intact nuclei have been isolated from cells of a diploid strain of Saccharomyces cerevisiae. The isolated nuclei were free from cytoplasmic, mitochondrial and vacuolar marker enzymes. The protein to DNA ratio (w/w) was 11. Pyrophosphatase, tripolyphosphatase and exopolyphosphatase activities have been found in S.
L P, Lichko +3 more
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Biokhimiia (Moscow, Russia), 1997
Saccharomyces cerevisiae mitochondria have a polyphosphatase activity which is insensitive to a number of inhibitors of mitochondrial ATPase and pyrophosphatase (PPase). Heparin (20 micrograms/ml) and EDTA (0.5 mM) do not inhibit ATPase and PPase activities but completely suppressed mitochondrial polyphosphatase activity.
L P, Lichko +2 more
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Saccharomyces cerevisiae mitochondria have a polyphosphatase activity which is insensitive to a number of inhibitors of mitochondrial ATPase and pyrophosphatase (PPase). Heparin (20 micrograms/ml) and EDTA (0.5 mM) do not inhibit ATPase and PPase activities but completely suppressed mitochondrial polyphosphatase activity.
L P, Lichko +2 more
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[Immunoenzyme analysis of polyphosphatases from various compartments of yeast cells].
Biokhimiia (Moscow, Russia), 1996Antibodies against purified polyphosphatase from the Saccharomyces cerevisiae cell envelope inhibited the activity of this enzyme and the polyphosphatase activity of the cytosol, being without any effect on vacuolar and nuclear polyphosphatase activities from the same yeast species cells.
T V, Kulakovskaia +3 more
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Biochemistry. Biokhimiia, 2000
A polyphosphatase with the specific activity 2.2 U/mg was purified to apparent homogeneity from a soluble preparation of mitochondria of Saccharomyces cerevisiae. The polyphosphatase is a monomeric protein of approximately 41 kD. The purified enzyme hydrolyzes polyphosphates with an average chain length of 9 to 208 phosphate residues to the same extent,
L P, Lichko +2 more
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A polyphosphatase with the specific activity 2.2 U/mg was purified to apparent homogeneity from a soluble preparation of mitochondria of Saccharomyces cerevisiae. The polyphosphatase is a monomeric protein of approximately 41 kD. The purified enzyme hydrolyzes polyphosphates with an average chain length of 9 to 208 phosphate residues to the same extent,
L P, Lichko +2 more
openaire +1 more source

