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P1146

Sigma-Aldrich

Phosphatase, acide from potato

lyophilized powder, ≥3.0 units/mg solid

Synonyme(s) :

(Monoester orthophosphorique phosphohydrolase, optimum acide), Phosphatase acide from potato

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About This Item

Numéro CAS:
9001-77-8
Numéro de classification (Commission des enzymes):
3.1.3.2 (BRENDA, IUBMB)
Numéro CE :
232-630-9
Numéro MDL:
MFCD00131847
Code UNSPSC :
12352204
eCl@ss :
42010102
Nomenclature NACRES :
NA.54

Forme

lyophilized powder

Activité spécifique

≥3.0 units/mg solid

Poids mol.

69 kDa

Conditions d'expédition

wet ice

Température de stockage

−20°C

InChI

1S/C6H10O2/c1-3-4-8-5-6(2)7/h1,6-7H,4-5H2,2H3

Clé InChI

GZCWLCBFPRFLKL-UHFFFAOYSA-N

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Description générale

Acid phosphatase from potato is a phosphomonoesterase, which can appear in multiple molecular forms of similar molecular mass but with different isoelectric points.

Application

Acid phosphatase from potato has been used in a study to assess the potential allergenicity of novel gene products. It has also been used in a study to remove eight phosphate groups from casein at a pH of 7.0.
The activity of potato acid phosphatase in various surfactant medias was examined. Bis(2- ethylhexyl)sodium sulfosuccinate, Brij 35, and SDS at 3mM inhibited phosphatase activity while the surfactant cetyltrimethylammonium bromide enhanced activity.

Actions biochimiques/physiologiques

Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7.

Définition de l'unité

One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 4.8 at 37 °C.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

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

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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J Lalitha et al.
Biochemistry and molecular biology international, 41(4), 797-803 (1997-04-01)
The effect of three different classes of surfactants viz., anionic, cationic and neutral on catalytic activity of potato acid phosphatase (AcPase) was studied. Anionic surfactants bis(2-ethylhexyl) sodium sulfosuccinate (AOT) and sodium dodecyl sulfate (SDS) inhibited AcPase activity completely at 3
P P Waymack et al.
Archives of biochemistry and biophysics, 288(2), 621-633 (1991-08-01)
An acid phosphatase (orthophosphoric monoester phosphohydrolase, acid optimum; EC 3.1.3.2) isoenzyme from wheat germ was purified 7000-fold to homogeneity. The effect of wheat germ sources and their relationship to the isoenzyme content and purification behavior of acid phosphatases was investigated.
Sishuo Cao et al.
Regulatory toxicology and pharmacology : RTP, 63(2), 181-187 (2012-04-17)
With the development of genetically modified crops, there has been a growing interest in available approaches to assess the potential allergenicity of novel gene products. We were not sure whether Cry1C could induce allergy. We examined the protein with three
S I Tu et al.
Plant physiology, 88(1), 61-68 (1988-09-01)
Primary cell walls, free from cytoplasmic contamination were prepared from corn (Zea mays L.) roots and potato (Solanum tuberosum) tubers. After EDTA treatment, the bound acid phosphatase activities were measured in the presence of various multivalent cations. Under the conditions
H N Fernley et al.
The Biochemical journal, 107(2), 279-283 (1968-03-01)
1. A purified preparation of alkaline phosphatase from calf-intestinal mucosa was phosphorylated by (32)P-labelled PP(i) at a serine residue on the enzyme. Under the conditions employed, up to 0.15mum-labelled sites were obtained from 1mum-[(32)P]PP(i). 2. The phosphorylated enzyme was labile
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Protocoles

Enzymatic Assay of Acid Phosphatase (EC 3.1.3.2)

Enzymatic Assay of Acid Phosphatase (EC 3.1.3.2)

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