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关于此项目
经验公式(希尔记法):
C10H8NaO4P
化学文摘社编号:
分子量:
246.13
MDL number:
Beilstein/REAXYS Number:
1969493
NACRES:
NA.83
PubChem Substance ID:
UNSPSC Code:
12352204
EC Number:
238-452-8
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 3
ppe
dust mask type N95 (US), Eyeshields, Gloves
C Hipólito-Reis et al.
Scandinavian journal of clinical and laboratory investigation, 59(8), 593-606 (2000-02-26)
The importance of separation and identification of serum alkaline phosphatase (ALP; E.C. 3.1.3.1) fractions/isoenzymes has been frequently reported. Each serum ALP fraction/isoenzyme quantitation has both practical and theoretical importance. In the present work, serum was collected from Wistar rats and
José Mauro Granjeiro et al.
Journal of enzyme inhibition and medicinal chemistry, 17(5), 345-350 (2003-04-10)
Uric acid inhibited 50% of the activity of bovine kidney low molecular mass phosphotyrosine protein phosphatase at concentrations of 1.0, 0.4, 1.3, and 0.2 mM, respectively for p-nitrophenyl phosphate (p-NPP), flavine mononucleotide, beta-naphthyl phosphate and tyrosine phosphate (Tyr-P) as substrates.
A Buist et al.
Biochemistry, 38(3), 914-922 (1999-01-20)
Most transmembrane, receptor-like protein-tyrosine phosphatases (RPTPs) contain two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains, of which the membrane-proximal domain, D1, contains the majority of the activity, while the membrane-distal domain, D2, exhibits little or no activity. We have investigated the
J M Granjeiro et al.
Biochemistry and molecular biology international, 41(6), 1201-1208 (1997-05-01)
A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0.
Liangsheng Wang et al.
Bio-protocol, 7(7), e2202-e2202 (2017-04-05)
Induction and secretion of acid phosphatase (APase) is a universal adaptive response of higher plants to low-phosphate stress ( Tran et al., 2010 ). The intracellular APases are likely involved in the remobilization and recycling of phosphate (Pi) from intracellular
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