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Merck

P1146

Phosphatase, Acid from potato

lyophilized powder, ≥3.0 units/mg solid

Synonym(s):

(Orthophosphoric-monoester phosphohydrolase acid optimum), Acid Phosphatase from potato

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About This Item

CAS Number:
9001-77-8
eCl@ss:
42010102
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-630-9
MDL number:
MFCD00131847
EC Number:
3.1.3.2 (BRENDA, IUBMB)

Key Documents

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Product Name

Phosphatase, Acid from potato, lyophilized powder, ≥3.0 units/mg solid

SMILES string

O(CC(O)C)CC#C

InChI key

GZCWLCBFPRFLKL-UHFFFAOYSA-N

InChI

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

form

lyophilized powder

specific activity

≥3.0 units/mg solid

mol wt

69 kDa

shipped in

wet ice

storage temp.

−20°C

Quality Level

300

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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.

Biochem/physiol Actions

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.

General description

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

Other Notes

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000502900
0000502899
0000502900
0000502899
0000444411

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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
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
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
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.
Y Sugiura et al.
The Journal of biological chemistry, 256(20), 10664-10670 (1981-10-25)
A new manganese-containing acid phosphatase has been isolated and crystallized from sweet potato tubers. The pure enzyme contains one atom of manganese per Mr = 110,000 polypeptide and shows phosphatase activity toward various phosphate substrates. The pH optimum of the
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Protocols

Enzymatic Assay of Acid Phosphatase (EC 3.1.3.2)

Enzymatic Assay of Acid Phosphatase (EC 3.1.3.2)

酸性磷酸酶的酶促测定（EC 3.1.3.2）

在测定酸性磷酸酶活性时，本操作流程使用对硝基苯基磷酸盐进行比色法测定。酶活性是使用分光光度计在410 nm处测定的。

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