SRE0048
酸性磷酸酶 来源于马铃薯
Suitable for manufacturing of diagnostic kits and reagents
别名:
(Orthophosphoric-monoester phosphohydrolase acid optimum), 酸性磷酸酶 来源于马铃薯
产品名称
酸性磷酸酶 来源于马铃薯, Suitable for manufacturing of diagnostic kits and reagents
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
form
lyophilized powder
specific activity
3.0-10.0 unit/mg solid
shipped in
wet ice
storage temp.
−20°C
Quality Level
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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.
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
E W Bingham et al.
Biochimica et biophysica acta, 429(2), 448-460 (1976-04-08)
Potato acid phosphatase (EC 3.1.3.2) was used to remove the eight phosphate groups from alphas1-casein. Unlike most acid phosphatases, which are active at pH 6.0 or below, potato acid phosphatase can catalyze the dephosphorylation of alphas1-casein at pH 7.0. Although
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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