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P1435

Sigma-Aldrich

Phosphatase, Acid from sweet potato

ammonium sulfate suspension, ≥10.0 units/mg protein (modified Warburg-Christian)

Synonym(s):

(Orthophosphoric-monoester phosphohydrolase [acid optimum] )

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About This Item

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

form

ammonium sulfate suspension

Quality Level

300

specific activity

≥10.0 units/mg protein (modified Warburg-Christian)

secondary activity

≤9.9 units/mg protein ATPase

mol wt

110 kDa

storage temp.

2-8°C

InChI

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

InChI key

GZCWLCBFPRFLKL-UHFFFAOYSA-N

General description

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

Application

Potato acid phosphatase is used as a dephosphorylating reagent in thiochrome assays for the detection of thiamin in biological samples. In this assay, it was shown to be more effective than acid phosphatases from wheat germ or α-amylase.
Sweet potato acid phosphatase has been used in a study as a pre-column enzyme reactor via a covalent bond with glutaraldehyde and aminopropyl controlled-pore glass. It has also been used in a study to investigate the use of tyrosine, histidine, and cysteine as ligands for Mn(III) in sweet potato phosphatase.

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 by the following reaction: APaseR-PO4 + H2O --------------- R-OH + HOPO3 2+Their function in the production, transport, and recycling of phosphate is critical for the metabolic and energy transduction processes of the cell. As a group, Apases may be as important as kinases in regulatory processes.

Unit Definition

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

Physical form

Suspension in 1.8 M (NH4)2SO4, 10 mM MgCl2, pH 5.3

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P1435-100UN:
P1435-500UN:
P1435-2.5KU:
P1435-VAR:
P1435-BULK:

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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S M Duff et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(21), 9538-9542 (1991-11-01)
Induction of phosphatase activity is an important component of the plant cell response to phosphate deficiency. Suspension cell cultures of Brassica nigra contain two major inducible acid phosphatase (APase) isozymes; vacuolar phosphoenolpyruvate (PEP) APase and cell wall nonspecific APase. Polyclonal
H Kawabe et al.
Biochimica et biophysica acta, 784(1), 81-89 (1984-01-18)
The function of Mn(III) in plant acid phosphatase has been investigated by a metal-substitution study, and some properties of the Fe(III)-substituted enzyme were compared with those of the native Mn(III) enzyme and mammalian Fe(III)-containing acid phosphatases. 19F nuclear magnetic resonance
G Schenk et al.
Archives of biochemistry and biophysics, 370(2), 183-189 (1999-10-08)
Purple acid phosphatases comprise a family of binuclear metal-containing acid hydrolases, representatives of which have been found in animals, plants, and fungi. The goal of this study was to characterize purple acid phosphatases from sweet potato tubers and soybean seeds
D T Wyatt et al.
Clinical chemistry, 35(11), 2173-2178 (1989-11-01)
We analyzed extensively a modified thiochrome method for thiamin analysis. Acid phosphatase (EC 3.1.3.2) from potato was superior to either alpha-amylase or acid phosphatase from wheat germ as a dephosphorylating agent. Timing of cyanogen bromide exposure was important, but the
Tatsuya Kusudo et al.
Bioscience, biotechnology, and biochemistry, 67(7), 1609-1611 (2003-08-13)
Purple acid phosphatase (PAP) was purified from sweet potato dry powder, which is used as a food additive. Spectrometric and enzymatic analyses, and analysis of the amino-terminal sequence indicated that the purified purple acid phosphatase was PAP1. High activity in
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