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Key Documents

A2230

Sigma-Aldrich

Apyrase from potatoes

High Activity, ATPase ≥600 units/mg protein, lyophilized powder

Synonyme(s) :

Adénosine 5′-diphosphatase, Adénosine 5′-triphosphatase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

potato

Forme

lyophilized powder

Qualité

High Activity

ATPase activity

≥600 units/mg protein

secondary activity

≥50 % of base activity ADPase

Composition

protein, ≥30%

Activité étrangère

Acid Phosphatase ≤2% of base activity

Conditions d'expédition

wet ice

Température de stockage

−20°C

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Application

Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation . Product A2230 is a high activity apyrase.
Au moins deux isoenzymes sont présentes dans diverses souches de S. tuberosum : l′une avec un rapport ATPase/ADPase élevé (∼ 10) et l′autre avec un rapport faible (∼ 1).
Réaction : ATP → ADP+Pi → AMP+2Pi.

Actions biochimiques/physiologiques

Apyrase is found in all eukaryotes and some prokaryotes. Apyrase, from potato, has a crucial role in regulating growth and development. Apyrase is involved in the inactivation of synaptic ATP as a neurotransmitter following nerve stimulation and in the inhibition of ADP induced platelet aggregation to prevent thrombosis . Divalent metal ions are required for activity and best activity is observed with calcium ion at 5 mM.

Conditionnement

Sold on the basis of ATPase units.

Définition de l'unité

One unit will liberate 1.0 μmole of inorganic phosphate from ATP or ADP per min at pH 6.5 at 30 °C.

Forme physique

Lyophilized powder containing potassium succinate buffer salts.

Notes préparatoires

Derived from red potato

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Mathieu F Chevalier et al.
Blood, 121(1), 29-37 (2012-10-09)
Natural regulatory T cells (Tregs) participate in responses to various chronic infections including HIV. HIV infection is associated with a progressive CD4 lymphopenia and defective HIV-specific CD8 responses known to play a key role in the control of viral replication.
Nicholas J Roberts et al.
Plant physiology, 161(1), 556-567 (2012-11-09)
Nodulation in legumes requires the recognition of rhizobially made Nod factors. Genetic studies have revealed that the perception of Nod factors involves LysM domain receptor-like kinases, while biochemical approaches have identified LECTIN NUCLEOTIDE PHOSPHOHYDROLASE (LNP) as a Nod factor-binding protein.
Tsan-Yu Chiu et al.
Plant & cell physiology, 53(11), 1913-1925 (2012-10-05)
Nucleoside triphosphate diphosphohydrolases (NTPDases; apyrases) (EC 3.6.1.5) hydrolyze di- and triphosphate nucleotides, but not monophosphate nucleotides. They are categorized as E-type ATPases, have a broad divalent cation (Mg(2+), Ca(2+)) requirement for activation and are insensitive to inhibitors of F-type, P-type
Ana Carolina Ribeiro Gomes Maia et al.
Parasitology international, 62(1), 44-52 (2012-09-22)
We identified a shared B domain within nucleoside triphosphate diphosphohydrolases (NTPDases) of plants and parasites. Now, an NTPDase activity not affected by inhibitors of adenylate kinase and ATPases was detected in Leishmania infantum promastigotes. By non-denaturing gel electrophoresis of detergent-homogenized
Gabriane Nascimento Porcino et al.
Experimental parasitology, 132(2), 293-299 (2012-08-28)
Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. In this work, mouse polyclonal antibodies produced against two synthetic peptides derived

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