P1146
Phosphatase, Acid from potato
lyophilized powder, ≥3.0 units/mg solid
Synonym(s):
(Orthophosphoric-monoester phosphohydrolase acid optimum), Acid Phosphatase from potato
form
lyophilized powder
Quality Level
specific activity
≥3.0 units/mg solid
mol wt
69 kDa
shipped in
wet ice
storage temp.
−20°C
SMILES string
O(CC(O)C)CC#C
InChI
1S/C6H10O2/c1-3-4-8-5-6(2)7/h1,6-7H,4-5H2,2H3
InChI key
GZCWLCBFPRFLKL-UHFFFAOYSA-N
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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.
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.
Other Notes
One unit will hydrolyze 1.0 μmole of p-nitrophenyl phosphate per min at pH 4.8 at 37 °C.
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
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
动植物源性产品
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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.
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
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
Mariusz Olczak et al.
Acta biochimica Polonica, 50(4), 1245-1256 (2004-01-24)
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal ligation. Animal PAPs contain a binuclear
Protocols
Enzymatic Assay of Acid Phosphatase (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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