Kinetic studies and properties of potato apyrase

Traverso-Cori, A.; Chaimovich, Hernán; Cori, Osvaldo

doi:10.1016/0003-9861(65)90303-6

Cited by 97 publications

(33 citation statements)

References 18 publications

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“…3A), and also an earlier observation that ATP was stoichiometrically converted to AMP when determinations were delayed by 2.5 hr after ATP assays (Fig. IB) (17). These characteristics of apyrase are similar to those of our factor, but our data were inconclusive as to whether our factor is identical with potato apyrase or composed of more than one isoenzyme.…”

Section: Resultssupporting

confidence: 84%

Possible Interference by an Acid-stable Enzyme during the Extraction of Nucleoside Di- and Triphosphates from Higher Plant Tissues

Ikuma¹,

Tetley²

1976

Plant Physiol.

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MATERIALS AND METHODSAcid extracts from tissues of two solanaceous plants were found to contain a heat-labile, nondialyzable factor which hydrolyzes nucleoside di-and triphosphates to nucleoside monophosphates. This acid-resistant factor shows optimal ATP-hydrolyzing activity at pH 5, whereas practically no activity was detected below pH 3 and above pH 9. It does not hydrolyze sugar phosphates, nucleoside monophosphates, uridine diphosphoglucose, and phosphoenolpyruvate. In order to estimate quantitatively the amount of nucleoside di-and triphosphates in a plant extract, care must be taken to circumvent possible interference by this factor. This is achieved by carefully maintaining the extract below pH 3.A method commonly employed for quantitative analysis of metabolic intermediates and products from animal tissues includes (a) quick fixation of tissue by freezing; (b) extraction and deproteination of frozen tissue with perchloric acid; (c) adjustment of the pH of extracts to near neutrality with KOH or K2CO3; and (d) quantitative determination of intermediates in neutralized extracts with a sensitive technique (1, 21). Similar procedures have been employed for extraction from plant tissues, where the intermediates have been frequently assayed with chromatographic techniques (4, 8, 9, 11, 13). Some investigators claim that this simple, rapid sampling and assay technique is not applicable to higher plant tissues because of possible degradation of labile phosphate esters in acid extracts (3,5,20), possible co-precipitation of phosphate esters with potassium perchlorate (2, 3), and difficulty in resolving these esters chromatographically (3, 5). Inability of acid to destroy some enzymes completely (6, 7, 21) may lead to erroneous results, when the acid extraction procedures are used.In our studies with tobacco pith tissue (16), where direct enzymic analyses of intermediate compounds (cf. 1, 21) were performed on extracts prepared with ethanolic formic acid (cf. 5), quantitative recoveries of ATP and ADP were not as satisfactory as those obtained from extracts prepared with formic or perchloric acid alone. Acid extracts, however, showed a timedependent destruction of ATP after their preparation. For this reason, several parameters associated with acid extraction of higher plant tissues were examined carefully. This communication reports a simple metlhod for avoiding the activity of the adenosine di-and triphosphate-destroying factor in acid extracts. ' Present address:

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Section: Resultssupporting

confidence: 84%

Possible Interference by an Acid-stable Enzyme during the Extraction of Nucleoside Di- and Triphosphates from Higher Plant Tissues

Ikuma¹,

Tetley²

1976

Plant Physiol.

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“…The activity assay was based on the method of Traverso-Cori et al (1965) with modifications. The reaction volumes were scaled down from 2 mL to 200 mL.…”

Section: Assays Of In Vitro Pollen Growth and Atp Level In Growth Mediummentioning

confidence: 99%

Apyrases (Nucleoside Triphosphate-Diphosphohydrolases) Play a Key Role in Growth Control in Arabidopsis

et al. 2007

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Expression of two Arabidopsis (Arabidopsis thaliana) apyrase (nucleoside triphosphate-diphosphohydrolase) genes with high similarity, APY1 and APY2, was analyzed during seedling development and under different light treatments using b-glucuronidase fusion constructs with the promoters of both genes. As evaluated by b-glucuronidase staining and independently confirmed by other methods, the highest expression of both apyrases was in rapidly growing tissues and/or tissues that accumulate high auxin levels. Red-light treatment of etiolated seedlings suppressed the protein and message level of both apyrases at least as rapidly as it inhibited hypocotyl growth. Adult apy1 and apy2 single mutants had near-normal growth, but apy1apy2 doubleknockout plants were dwarf, due primarily to reduced cell elongation. Pollen tubes and etiolated hypocotyls overexpressing an apyrase had faster growth rates than wild-type plants. Growing pollen tubes released ATP into the growth medium and suppression of apyrase activity by antiapyrase antibodies or by inhibitors simultaneously increased medium ATP levels and inhibited pollen tube growth. These results imply that APY1 and APY2, like their homologs in animals, act to reduce the concentration of extracellular nucleotides, and that this function is important for the regulation of growth in Arabidopsis.

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“…Actually, the existence of the potato apyrase has been known for decades before its cloning, and the first effort in isolating the protein was reported more than 60 years ago [128]. This was followed by many published studies from the laboratory of Traverso-Cori on the potato apyrase isoforms and their biochemical properties [17,129,130]. It is marketed by Sigma and is widely used in experiments when rapid elimination of ATP is needed.…”

Section: Plantsmentioning

confidence: 99%

The GDA1_CD39 superfamily: NTPDases with diverse functions

Knowles

2011

Purinergic Signalling

145

117

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The first comprehensive review of the ubiquitous "ecto-ATPases" by Plesner was published in 1995. A year later, a lymphoid cell activation antigen, CD39, that had been cloned previously, was shown to be an ecto-ATPase. A family of proteins, related to CD39 and a yeast GDPase, all containing the canonical apyrase conserved regions in their polypeptides, soon started to expand. They are now recognized as members of the GDA1_CD39 protein family. Because proteins in this family hydrolyze nucleoside triphosphates and diphosphates, a unifying nomenclature, nucleoside triphosphate diphopshohydrolases (NTPDases), was established in 2000. Membrane-bound NTPDases are either located on the cell surface or membranes of intracellular organelles. Soluble NTPDases exist in the cytosol and may be secreted. In the last 15 years, molecular cloning and functional expression have facilitated biochemical characterization of NTPDases of many organisms, culminating in the recent structural determination of the ecto-domain of a mammalian cell surface NTPDase and a bacterial NTPDase. The first goal of this review is to summarize the biochemical, mutagenesis, and structural studies of the NTPDases. Because of their ability in hydrolyzing extracellular nucleotides, the mammalian cell surface NTPDases (the ecto-NTPDases) which regulate purinergic signaling have received the most attention. Less appreciated are the functions of intracellular NTPDases and NTPDases of other organisms, e.g., bacteria, parasites, Drosophila, plants, etc. The second goal of this review is to summarize recent findings which demonstrate the involvement of the NTPDases in multiple and diverse physiological processes: pathogen-host interaction, plant growth, eukaryote cell protein and lipid glycosylation, eye development, and oncogenesis.

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Kinetic studies and properties of potato apyrase

Cited by 97 publications

References 18 publications

Possible Interference by an Acid-stable Enzyme during the Extraction of Nucleoside Di- and Triphosphates from Higher Plant Tissues

Possible Interference by an Acid-stable Enzyme during the Extraction of Nucleoside Di- and Triphosphates from Higher Plant Tissues

Apyrases (Nucleoside Triphosphate-Diphosphohydrolases) Play a Key Role in Growth Control in Arabidopsis

The GDA1_CD39 superfamily: NTPDases with diverse functions

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