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The enzyme alkaline phosphatase (ALP, alkaline phenyl phosphatase, also abbreviated PhoA) is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found ...
5-Bromo-4-chloro-3-indolyl phosphate (BCIP, X-phosphate, XP) is an artificial chromogenic substrate used for the sensitive colorimetric detection of alkaline phosphatase activity. It is, for example, used in immunoblotting , in situ hybridization , and immunohistochemistry , often in combination with nitro blue tetrazolium chloride (NBT).
However, when experiments have been carried out in-vivo, phosphatase enzymes have been shown to be incredibly specific. [3] In some cases, a protein phosphatase (i.e. one defined by its recognition of protein substrates) can catalyze the dephosphorylation of nonprotein substrates. [ 4 ]
Specific activity gives a measurement of enzyme purity in the mixture. It is the micro moles of product formed by an enzyme in a given amount of time (minutes) under given conditions per milligram of total proteins. Specific activity is equal to the rate of reaction multiplied by the volume of reaction divided by the mass of total protein.
ALP activity is significantly increased in the third trimester of pregnancy. [11] This is due to increased synthesis from the placenta as well as increased synthesis in the liver induced by large amounts of estrogens. [11] [12] [13] Levels in the third trimester can be as much as 2-fold greater than in non-pregnant women. [11]
The relative activity of a species i, denoted a i, is defined [4] [5] as: = where μ i is the (molar) chemical potential of the species i under the conditions of interest, μ o i is the (molar) chemical potential of that species under some defined set of standard conditions, R is the gas constant, T is the thermodynamic temperature and e is the exponential constant.
This property can be used to determine the activity of various phosphatases including alkaline phosphatase (AP) and protein tyrosine phosphatase (PTP). [ 3 ] PNPP is classified as a chromogenic substrate because of its ability to transform from a colorless compound to a colored compound through a biological mechanism, dephosphorylation. [ 4 ]
The method combines the reactions of copper ions with the peptide bonds under alkaline conditions (the Biuret test) with the oxidation of aromatic protein residues. The Lowry method is based on the reaction of Cu +, produced by the oxidation of peptide bonds, with Folin–Ciocalteu reagent (a mixture of phosphotungstic acid and phosphomolybdic acid in the Folin–Ciocalteu reaction).