Nucleoside diphosphokinase from beef heart mitochondria. Purification and properties

Colomb, Maurice G.; Chéruy, A.; Vignais, Pierre V.

doi:10.1021/bi00833a024

Cited by 43 publications

(7 citation statements)

References 40 publications

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“…Enzyme Assays. An isotopic test (Colomb et al, 1969) was used for kinetic studies. In routine assays, the incubation medium consisted of 6 mM ATP, 12 mM MgCl2, 0.2 mM [32P]ADP, and 0.1 m triethanolamine-HCI buffer (pH 8.0) (standard incubation medium).…”

Section: Methodsmentioning

confidence: 99%

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Colomb¹,

Chéruy²,

Vignais³

et al. 1974

Biochemistry

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Section: Methodsmentioning

confidence: 99%

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Colomb¹,

Chéruy²,

Vignais³

et al. 1974

Biochemistry

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“…This was not due to enhanced ADP dephosphorylation since the concentration of AMP + adenosine did not change much by addition of ATP (Table 4, experiment III). However, the increased reduction in 3 H-ADP after incubation was reflected by a nearly corresponding increase in radioactive ATP, indicating the presence of nucleoside diphosphokinase, an enzyme especially reactive towards ADP ( 1).…”

Section: Specificity Of the Adpasementioning

confidence: 96%

Partial Purification and Characterization of an ADP Phosphohydrolase from Human Plasma

Holmsen¹,

Holmsen²

1971

Thromb Haemost

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SummaryPlasma contains enzymes capable of dephosphorylating ADP, ATP and AMP (adenosine di-, tri- and monophosphate). In platelet-rich plasma these enzymes are important for the regulation of the levels of (platelet-aggregating) ADP and (aggregation-inhibitory) adenosine.Plasma ADPase and ATPase were studied at 1 (µM substrate concentration using an isotope technique. Both enzymes were precipitated from plasma at 45-65% saturation with (NH4)2S04 and emerged together by gel filtration on Sephadex G-200 and from DEAE-Sephadex (0.12-0.20 M Cl-, pH 8.2). In combination these procedures gave 1,500-1,800 times purification of ADPase relative to plasma. The purest fraction contained ATPase, ADPase and AMPase in a 0.17:1.00:2.92 proportion, quite different from their 5.34:1.00:5.34 proportion in plasma. Adenosine deaminase and adenylate kinase were not present in the purest fraction, whereas nucleoside diphosphokinase appeared to be present.The purified ADPase was stimulated by low concentrations of Mg2+ and Mn2+, whereas high concentrations were inhibitory. This inhibition could not be explained by an increase in the ionic strength. Ca2+ and Zn2+ were inhibitory at all concentrations used (0-3 mM). Lineweaver-Burke plots were linear for both ADPase and ATPase in the 0−4 x 10-5 M substrate range, and both enzymes had Km = 1.1 x 10−5 M. Increase of the substrate concentration above 4 x 10−5M gave deviation from MichaelisMenten kinetics, and Eadie-Hofstee plots indicated the presence of “high-Km” ADPase and ATPase. The latter enzymes were not studied.Déphosphorylation of 3H-ADP by purified “low-Km” ADPase was reduced by nonradioactive diphosphates of guanosine, inosine, cytidine and uridine in the same way as when nonradioactive ADP was used. Nonradioactive AMP also reduced dephosphorylation of 3H-ADP, whereas nonradioactive ATP did not.Cyanide, cysteine and tartrate inhibited “low-Km” ADPase whereas p-chloromercuribenzoate, p-chloromercuribenzoesulphonate and N-ethylmaleimide had no effect. EDTA inhibited the enzyme activity in a way that could not be abolished by excess Mg2+. Purified plasma “low-Km” ADPase thus appears to be an unspecific enzyme, as one and the same active site does not seem to distinguish between the base moiety of nucleoside diphosphates, and catalyzes hydrolysis of phosphate esters as well as pyrophosphate bonds. The relation between plasma ADPase and ATPase remains unclear.

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“…Cygb, a kind of porphyrin ring shows catalase activity in hepatic stellate cells, which play a role in peroxide scavenger [33]. NDPK-A, a multifunctional protein, can regulate metabolism, cell proliferation, and differentiation [34]. Although these proteins have various biological functions, their functions in liver injury have been rarely reported before.…”

Section: Discussionmentioning

confidence: 99%

Application of Proteomic and Bioinformatic Techniques for Studying the Hepatoprotective Effect of Dioscin against CCl₄-induced Liver Damage in Mice

Yin

Li-na

et al. 2010

Planta Med

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In this study, the significant hepatoprotective effect of dioscin against CCl₄-induced acute liver damage in mice was first discovered, and the effect produced by dioscin at the dose of 100 mg/kg was equal to the action produced by silymarin at the dose of 200 mg/kg. Then, 1-dimension gel electrophoresis was used to separate the liver proteins, and five differentially expressed bands were selected. After in-gel digestion, 71 proteins were identified by nano-RP-HPLC-ESI-MS/MS/MS. Further network analysis suggested that the identified proteins formed a connected protein interaction subnetwork. Ten functional categories were selected to demonstrate the distribution of the proteins by Gene Ontology (GO) enrichment analysis. Six of the proteins, heat shock protein 5 (HSPA5), annexin 6 (ANXA6), isovaleryl-CoA dehydrogenase (IVD), ribosomal protein S6 (RPS6), cytoglobin (Cygb), and nucleoside diphosphate kinase A (NDPK-A), were validated by Western blotting assay. They might be involved in the hepatoprotective effect of dioscin, and their investigation could be useful, together with the determination of serum alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), and lactate dehydrogenase (LDH) levels, as well as the liver histopathologic study, for the elucidation of the action mechanisms of dioscin against CCl₄-induced liver injury. Our work shows that the validated proteins should be considered as biomarkers for the investigation of acute liver injury, and its results should contribute to the therapy of liver damage by dioscin in the future.

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Nucleoside diphosphokinase from beef heart mitochondria. Purification and properties

Cited by 43 publications

References 40 publications

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Partial Purification and Characterization of an ADP Phosphohydrolase from Human Plasma

Application of Proteomic and Bioinformatic Techniques for Studying the Hepatoprotective Effect of Dioscin against CCl₄-induced Liver Damage in Mice

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Nucleoside diphosphokinase from beef heart mitochondria. Purification and properties

Cited by 43 publications

References 40 publications

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Adenosine diphosphate as a regulatory ligand in beef heart cytosol nucleoside diphosphokinase

Partial Purification and Characterization of an ADP Phosphohydrolase from Human Plasma

Application of Proteomic and Bioinformatic Techniques for Studying the Hepatoprotective Effect of Dioscin against CCl4-induced Liver Damage in Mice

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Product

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About

Application of Proteomic and Bioinformatic Techniques for Studying the Hepatoprotective Effect of Dioscin against CCl₄-induced Liver Damage in Mice