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A6410

Sigma-Aldrich

Apyrase from potatoes

ATPase ≥200 units/mg protein, lyophilized powder

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Synonym(s):
Adenosine 5′-diphosphatase, Adenosine 5′-triphosphatase
CAS Number:
9000-95-7
Enzyme Commission number:
3.6.1.5 (BRENDA, IUBMB)
EC Number:
232-569-8
MDL number:
MFCD00130542
NACRES:
NA.54

type

Grade VI

Quality Level

200

form

lyophilized powder

ATPase activity

≥200 units/mg protein

secondary activity

≤15 % of base activity ADPase

mol wt

~49 kDa by gel filtration

composition

Protein, 30-60%

solubility

H2O: soluble 1.0 mg/mL

foreign activity

Acid Phosphatase ≤2% of base activity

storage temp.

−20°C

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General description

Apyrase, also known as ATP-diphosphohydrolase, is expressed in wide variety of plant and animal tissues. The commercially accessible apyrase enzyme is isolated from potato tubers.

Application

Apyrase from potatoes has been used:
  • to deplete ATP
  • to degrade endogenous extracellular ATP
  • as a supplement in acid citrate dextrose solution to treat blood obtained from anesthetized mice

Apyrase is used to hydrolyze nucleoside triphosphates and diphosphates. For hydrolysis of organic di and triphosphates, the optimal pH is 6, and for inorganic substrates, the optimal pH is 5.1. Apyrase, from Sigma, has been used in inhibition studies of platelet-aggregation .
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 hydrolyses the phosphoanhydride bonds of nucleoside tri- and di-phosphates in the presence of divalent cations. It has wide substrate specificity for nucleotides. This property of the enzyme makes it suitable for different biotechnical applications, including DNA sequencing and platelet-aggregation inhibition. Apyrase has adenosine 5′-triphosphatase (ATPase) and adenosine 5′-diphosphatase (ADPase) activities.
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.

Other Notes

This grade has an exceptionally high ATPase/ADPase ratio.

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

Partially purified, lyophilized powder containing potassium succinate buffer salts.

Preparation Note

Derived from white potato

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Micromanipulation studies of chromatin fibers in Xenopus egg extracts reveal ATP-dependent chromatin assembly dynamics
Yan J, et al.
Molecular Biology of the Cell, 18(2), 464-474 (2007)
Surfactant inhibits ATP-induced release of interleukin-1beta via nicotinic acetylcholine receptors
Backhaus S, et al.
Journal of Lipid Research, 58(6), 1055-1066 (2017)
Stefan Golfier et al.
eLife, 9 (2020-05-13)
Loop extrusion by structural maintenance of chromosomes (SMC) complexes has been proposed as a mechanism to organize chromatin in interphase and metaphase. However, the requirements for chromatin organization in these cell cycle phases are different, and it is unknown whether
Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum).
Nourizad N, et al.
Protein Expression and Purification, 27(2), 229-237 (2003)
Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1.
Smith T M & Kirley T L
Biochimica et Biophysica Acta, 1386(1), 65-78 (1998)
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