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A2230

Sigma-Aldrich

Apyrase from potatoes

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

Synonym(s):

Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

potato

Quality Level

form

lyophilized powder

quality

High Activity

ATPase activity

≥600 units/mg protein

secondary activity

≥50 % of base activity ADPase

composition

protein, ≥30%

foreign activity

Acid Phosphatase ≤2% of base activity

shipped in

wet ice

storage temp.

−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.
At least two isoenzymes are found in different varieties of S. tuberosum: one with a high ATPase/ADPase ratio (∼10) and another with a low ratio (∼1).
Reaction: ATP → ADP+Pi → AMP+2Pi.

Biochem/physiol Actions

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.

Packaging

Sold on the basis of ATPase units.

Unit Definition

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

Physical form

Lyophilized powder containing potassium succinate buffer salts.

Preparation Note

Derived from red potato

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Yong Zhang et al.
Transplant immunology, 27(4), 175-178 (2012-08-14)
To study the effects and mechanisms of the imbalance in B cell-expressed nucleoside triphosphate diphosphohydrolase 1 (NTPDase 1)-induced ADP degradation on graft injury during acute antibody-mediated rejection (AMR). The acute AMR animal model was established in male NTPDase 1-wild-type Balb/c
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
Maja Milošević et al.
Molecular and cellular biochemistry, 371(1-2), 199-208 (2012-09-08)
Extracellular nucleotides affect female reproductive functions, fertilization, and pregnancy. The aim of this study was to investigate biochemical characteristics of ATP and ADP hydrolysis and identify E-NTPDases in myometrial cell membranes from Wistar albino rats. The apparent K (m) values
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

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