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Higher-plant cyclic nucleotide phosphodiesterases. Resolution, partial purification and properties of three phosphodiesterases from potato tuber.

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1. Three phosphodiesterases that are capable of hydrolysing 3':5'-cyclic nucleotides were purified from potato tubers. 2. The phosphodiesterases were fractionated by (NH4)2SO4 precipitation and CM-cellulose chromatography. The phosphodiesterases were resolved from each other and further purified by

Identification of the 3' 5' - cyclic AMP phosphodiesterase inhibitor in potato: feed-back control by inorganic phosphate.

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Evidence for and some properties of a 3', 5'-cyclic AMP phosphodiesterase inhibitor in potato.

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Purification of a ribonuclease from potato tubers and its use as an antigen in the immunochemical assay of this protein following tuber damage.

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A method for the purification of a ribonuclease from potato tubers is described. The preparation was free from deoxyribonuclease and phosphodiesterase activities and possessed only slight phosphomonoesterase activity. Specific antibodies against the ribonuclease preparation were raised in rabbits.

Use of potato tuber nucleotide pyrophosphatase to synthesize adenosine 5'-monophosphate methyl ester: evidence that the solvolytic preferences of the enzyme are regulated by pH and temperature.

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Nucleotide alkyl esters are pharmacologically important as potential (ant)agonists of purinoceptors and inhibitors of enzymes. Potato nucleotide pyrophosphatase (PNP) was compared with snake venom phosphodiesterase (SVP) as a catalyst to synthesize nucleotide alkyl esters. In methanol-water

Isolation and properties of lysosomes from dark-grown potato shoots.

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A method is described for the isolation of lysosomal fractions from dark-grown potato shoots using a single stage separation on a Ficoll gradient. Peaks of acid hydrolase activity consisting of acid phosphatase, phosphodiesterase, ribonuclease, carboxylic esterase and β-glycerophosphatase were well

Histochemical localization of nucleotide pyrophosphatase and cyclic nucleotide phosphodiesterase in seeds and shoots of Triticum.

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The activities of potato nucleotide pyrophosphatase and cyclic nucleotide phosphodiesterase against a common substrate, p-nitrophenyl thymidine 5'-phosphate and its histochemical analogue, AS-BI-naphthyl thymidine 5'-phosphate, were determined with the aid of relatively specific inhibitors, NAD and

Increase in ribonuclease activity following mechanical damage to leaf and tuber tissues of Solanum tuberosum L.

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Major increases occurred in the capacity of damaged potato leaf and tuber tissues to hydrolyse ribonucleic acid whilst relatively minor increases were found in the activity of acid phosphomonoesterase and acid phosphodiesterase. Partial purification of homogenates by gel filtration on Sephadex G-100

[The formation of stable aggrregates of human platelets induced by lectin from Solanum tuberosum].

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It has been demonstrated for the first time that GlcNAc-specific lectin from Solanum tuberosum induces the formation of haptenic sugar-resistant intercellular contacts (HSR-contacts) in platelet aggregation and does not induce stable neutrophil and lymphocyte aggregation. The formation of

Impact of potato cultivation and cattle farming on physicochemical parameters and enzymatic activities of Neotropical high Andean Páramo ecosystem soils.

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The Andean Páramos are high mountain ecosystems whose soils are essential for the management of South American water resources, but research on anthropic impacts to these soils is currently minimal and insufficient. The objective of this study was to evaluate the impacts of potato (Solanum

[Cytochemical localization and properties of selected nucleolytic enzymes].

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In the article there are shortly outlined studies on cytochemical localization of selected nucleolytic enzymes carried out between 1957-1986 by David Shugar and his coworkers. The histochemical localization of several nucleolytic enzymes in animal and plant tissues was determined by synthesis of

Effect of pressure on plant endonuclease reactions.

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Effect of pressure on plant endonucleases, nuclease P1 from penicillium and an endonuclease from potato, was investigated especially on the influence on phosphomonoesterase and phosphodiesterase activities shown on substrates of XpYp type, as well as their intrinsic pressure-stability. The potato

Characterization of transposon insertion out- mutants of Erwinia carotovora subsp. carotovora defective in enzyme export and of a DNA segment that complements out mutations in E. carotovora subsp. carotovora, E. carotovora subsp. atroseptica, and Erwinia chrysanthemi.

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Soft-rotting Erwinia spp. export degradative enzymes to the cell exterior (Out+), a process contributing to their ability to macerate plant tissues. Transposon (Tn5, Tn10, Tn10-lacZ) insertion Out- mutants were obtained in Erwinia carotovora subsp. carotovora 71 by using plasmid and bacteriophage

The structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like fold.

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Phosphatases function in the production, transport and recycling of inorganic phosphorus, which is crucial for cellular metabolism and bioenergetics, as well as in bacterial killing, since they are able to generate reactive oxygen species via Fenton chemistry. Diphosphonucleotide

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Herbal & Natural Medicine

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Интерактивна ГПС мапа - означите биље на локацији (ускоро)
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