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p-Nitrophenylphosphorylcholine Sale

(Synonyms: O-(对硝基苯基磷酰)胆碱) 目录号 : GC44664

A chromogenic PLC substrate

p-Nitrophenylphosphorylcholine Chemical Structure

Cas No.:21064-69-7

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产品描述

p-Nitrophenylphosphorylcholine is a chromogenic substrate that is used to measure phospholipase C (PLC) activity. Hydrolysis of p-nitrophenylphosphorylcholine by PLC results in the liberation of p-nitrophenol, which can be measured at 405 nm at pH 7.2-7.5.

Chemical Properties

Cas No. 21064-69-7 SDF
别名 O-(对硝基苯基磷酰)胆碱
Canonical SMILES C[N+](C)(C)CCOP(OC1=CC=C([N+]([O-])=O)C=C1)([O-])=O
分子式 C11H17N2O6P 分子量 304.2
溶解度 DMF: 1 mg/ml,DMSO: 10 mg/ml,Ethanol: 10 mg/ml,PBS (pH 7.2): 10 mg/ml 储存条件 Store at -20°C
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1 mM 3.2873 mL 16.4366 mL 32.8731 mL
5 mM 0.6575 mL 3.2873 mL 6.5746 mL
10 mM 0.3287 mL 1.6437 mL 3.2873 mL
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Research Update

Critical evaluation of p-Nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C*

Enzyme Microb Technol 2000 Mar 1;26(5-6):451-458.PMID:10713220DOI:10.1016/s0141-0229(99)00190-8.

Phospholipase C (PLC) activity secreted by bacteria as a virulence factor is commonly detected by use of the artificial substrate p-Nitrophenylphosphorylcholine (p-NPPC). We examined several commercially available enzymes (phosphodiesterases, phosphomonoesterases, phospholipase A, lipase, protease) for their hydrolytic activity towards p-NPPC and compared these results with those of PLC tests using phospholipid substrates. Our data indicate that, in addition to PLC, several other enzymes which can affect phosphate esters are able to hydrolyze p-NPPC. We therefore suggest to use lipid substrates for correct characterization of bacterial PLCs, especially when whole bacteria or crude enzyme preparations are investigated.

A spectrophotometric assay of Zn(2+)-glycerophosphorylcholine phosphocholine phosphodiesterase using p-Nitrophenylphosphorylcholine

Anal Biochem 1992 Jun;203(2):201-5.PMID:1384383DOI:10.1016/0003-2697(92)90303-o.

A direct spectrophotometric assay for the glycerophosphorylcholine phosphocholine phosphodiesterase requiring zinc ions for activity is described. This assay is based on the continuous measurement of p-nitrophenol produced from the enzymatic hydrolysis of p-Nitrophenylphosphorylcholine. The assay method, which showed a good linearity with time and amount of protein, was found to be rapid, simple, and, at the same time, accurate and sensitive enough to allow the quantitation of nanomolar amounts of product. With an alkaline buffer containing Triton X-100, the Zn(2+)-glycerophosphorylcholine phosphocholine phosphodiesterase activity in the tissue homogenate can be directly and selectively measured by this technique. The specific activity of the phosphodiesterase in brain and kidney was determined to be 80 and 6.5 nmol/h mg protein, respectively, and much lower activity was present in other tissues.

An unusual phosphodiesterase activity towards p-Nitrophenylphosphorylcholine present in rat brain membranes

Neurochem Res 1990 Oct;15(10):987-92.PMID:1963926DOI:10.1007/BF00965744.

A phosphodiesterase activity present in rat brain membranes has been examined utilizing p-Nitrophenylphosphorylcholine as the substrate. This enzyme activity has a pH optimum of 8.5, is stimulated by a variety of free fatty acids, requires either Zn+2 or Ca+2 and is relatively stable to heating at 75 degrees C for 7.5 minutes. These properties appear to distinguish this particular activity from those previously reported for alkaline phosphatase, nonspecific phosphodiesterase, phosphodiesterases I and II, lecithinase, and sphingomyelinase.

Selective chemical catalysis by an antibody

Science 1986 Dec 19;234(4783):1570-3.PMID:3787262DOI:10.1126/science.3787262.

The immunoglobulin MOPC167, which binds the transition state analog p-Nitrophenylphosphorylcholine with high affinity, catalyzed the hydrolysis of the corresponding carbonate 1. MOPC167 catalysis displayed saturation kinetics with catalytic constant (kcat) = 0.4 min-1 and Michaelis constant (Km) = 208 microM, showed substrate specificity, and was inhibited by p-Nitrophenylphosphorylcholine. The rate of the reaction was first order in hydroxide ion concentration between pH 6.0 and 8.0. The lower limit for the rate of acceleration of hydrolysis by the antibody above the uncatalyzed reaction was 770. This study begins to define the rules for the generation of catalytic antibodies.

Cytolytic and phospholipase C activity in Legionella species

J Gen Microbiol 1985 Jun;131(6):1383-91.PMID:4045420DOI:10.1099/00221287-131-6-1383.

To examine one possible mechanism of damage to leucocytes and tissue cells in legionellosis, seven species of Legionella were examined for cytolytic activity and for elaboration of phospholipase C, an enzyme that can damage mammalian cell membranes. Cytolysis was assessed using erythrocytes in agar. Phospholipase C was assayed by release of p-nitrophenol from p-Nitrophenylphosphorylcholine and of tritiated phosphorylcholine from L-alpha-dipalmitoyl-[choline-methyl-3H]phosphatidylcholine. L. pneumophila, L. bozemanii, L. micdadei, L. dumoffii, L. gormanii, L. longbeachae and L. jordanis all lysed dog red blood cells, which have a high ratio of membrane phosphatidylcholine to sphingomyelin. The same strains hydrolysed varying amounts of p-Nitrophenylphosphorylcholine; L. bozemanii exhibited the greatest activity. L. pneumophila, L. bozemanii, L. dumoffii, L. longbeachae and L. jordanis, but not L. micdadei, released tritiated phosphorylcholine from labelled substrate. These results indicate that several species of Legionella possess cytolytic capability; exotoxins with activity may play a role.