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3.1.3.2

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Klement Rejsek et al.
TheScientificWorldJournal, 2012, 250805-250805 (2012-06-16)
The aim of this study is to present a new method for determining the root-derived extracellular acid phosphomonoesterase (EAPM) activity fraction within the total EAPM activity of soil. EAPM activity was determined for roots, organic and mineral soil. Samples were...
W S Ostrowski et al.
Clinica chimica acta; international journal of clinical chemistry, 226(2), 121-129 (1994-05-01)
Human prostatic acid phosphatase (EC 3.1.3.2) is a non-specific phosphomonoesterase, synthetized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Gene coding this protein is localized on chromosome 3. Since...
E Dziembor-Gryszkiewicz et al.
Biochemistry international, 6(5), 627-633 (1983-05-01)
The acid phosphatase [EC 3.1.3.2] from human prostate gland is very unstable glycoprotein. To stabilize the enzyme cross-linking reaction with diamines was adopted. The carboxyl groups of the enzyme were activated with 1-ethyl-(3-dimethylaminopropyl)-carbodiimide and then treated with diamines of H2N-(CH2)n-NH2...
L Gianfreda et al.
Biotechnology and bioengineering, 26(5), 518-527 (1984-05-01)
Acid phosphatase (E.C.3.1.3.2.) thermal deactivation at pH 3.77 has been investigated by monitoring the enzyme activity as a function of time in the hydrolysis of p-nitrophenyl phosphate. The experimental curves obtained show a two-slope behavior in a log (activity)versus-time plot...
Yoshihiko Igarashi et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 781(1-2), 345-358 (2002-11-27)
Various biochemical markers have been used to assess bone metabolism and to monitor the effects of treatments. Tartrate resistant acid phosphatase (TRAP; EC 3.1.3.2) has often been used to assess bone absorption. Although osteoclasts contain abundant TRAP and they are...
P Hu et al.
Biochemical and biophysical research communications, 167(2), 520-527 (1990-03-16)
The catalytic and immunological properties of acid phosphatases (EC 3.1.3.2.) in different tissues were studied. It was demonstrated that high uptake forms of lysosomal enzymes like beta-galactosidase isolated from human platelets and bovine testis are mature enzymes, which have not...
J D Cooper et al.
Clinica chimica acta; international journal of clinical chemistry, 126(3), 297-306 (1982-12-23)
The estimation of acid phosphatase (EC 3.1.3.2) in serum by reaction rate analysis, utilising alpha-naphthyl phosphate as substrate and a diazonium salt (Fast Red TR) for colour development is examined. In the absence of substrate the occurrence of a pseudo...
M S Saini et al.
Biochimica et biophysica acta, 568(2), 370-376 (1979-06-06)
Treatment of homogenous human prostatic acid phosphatase (orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2) with low concentrations of Woodward's reagent K (N-ethyl-5-phenylisoxazolium-3'-sulfonate) leads to a rapid loss of enzymic activity. The rate of inactivation of the enzyme is reduced in the...
G C Irving et al.
Journal of bacteriology, 112(1), 434-438 (1972-10-01)
The fungus Aspergillus ficuum NRRL 3135 is known to produce an extracellular nonspecific orthophosphoric monoester phosphohydrolase (EC 3.1.3.2) with a pH optimum of 2.0, as well as an extracellular myo-inositol hexaphosphate phosphohydrolase (EC 3.1.3.8; phytase) with pH optima of 2.0...
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...
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...
R W Weber et al.
The Histochemical journal, 31(5), 293-301 (1999-08-26)
An integrated approach to acid phosphatase (EC 3.1.3.2) histochemistry by the azo-dye and lead-capture ('Gomori') methods in phosphate-starved hyphae of the fungus Botrytis cinerea revealed strikingly different patterns of localization of activity staining. Reaction product formed with the azo-dye method...
W J Wannet et al.
Antonie van Leeuwenhoek, 77(3), 215-222 (2004-06-11)
Acid phosphatase [AP; EC 3.1.3.2], a key enzyme involved in the synthesis of mannitol in Agaricus bisporus, was purified to homogeneity and characterized. The native enzyme appeared to be a high molecular weight type glycoprotein. It has a molecular weight...
R Senna et al.
Plant physiology and biochemistry : PPB, 44(7-9), 467-473 (2006-10-07)
Acid phosphatase activity (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) increased during the first 24 h of maize (Zea mays) seed germination. The enzyme displayed a pH optimum of 4.5-5.5. Catalytic activity in vitro displayed a linear time course (60 min) and reached...
M Barile et al.
European journal of biochemistry, 249(3), 777-785 (1997-12-12)
In order to gain some insight into mitochondrial flavin biochemistry, rat liver mitochondria essentially free of lysosomal and microsomal contamination were prepared and their capability to metabolise externally added and endogenous FAD and FMN tested both spectroscopically and via HPLC....
L L Shekels et al.
Protein science : a publication of the Protein Society, 1(6), 710-721 (1992-06-01)
We have partially purified an 18-kDa cytoplasmic protein from 3T3-L1 cells, which dephosphorylates pNPP and the phosphorylated adipocyte lipid binding protein (ALBP), and have identified it by virtue of kinetic and immunological criteria as an acid phosphatase (EC 3.1.3.2). The...
P Vihko et al.
FEBS letters, 236(2), 275-281 (1988-08-29)
lambda gt11 clones encoding human prostatic acid phosphatase (PAP) (EC 3.1.3.2) were isolated from human prostatic cDNA libraries by immunoscreening with polyclonal antisera. Sequence data obtained from several overlapping clones indicated that the composite cDNAs contained the complete coding region...
Maria Luigia Pallotta
Yeast (Chichester, England), 28(10), 693-705 (2011-09-15)
Despite the crucial roles of flavin cofactors in metabolism, we know little about the enzymes responsible for the turnover of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) and their subcellular localization. The mechanism by which mitochondria obtain their own...
P P Waymack et al.
Archives of biochemistry and biophysics, 288(2), 621-633 (1991-08-01)
An acid phosphatase (orthophosphoric monoester phosphohydrolase, acid optimum; EC 3.1.3.2) isoenzyme from wheat germ was purified 7000-fold to homogeneity. The effect of wheat germ sources and their relationship to the isoenzyme content and purification behavior of acid phosphatases was investigated....
R Pohlmann et al.
The EMBO journal, 7(8), 2343-2350 (1988-08-01)
A 2112-bp cDNA clone (lambda CT29) encoding the entire sequence of the human lysosomal acid phosphatase (EC 3.1.3.2) was isolated from a lambda gt11 human placenta cDNA library. The cDNA hybridized with a 2.3-kb mRNA from human liver and HL-60...
L Nguyen et al.
Clinical chemistry, 36(8 Pt 1), 1450-1455 (1990-08-01)
We developed an assay to measure at acid pH the phosphotyrosine phosphatase activity in sera from patients with prostatic cancer. The method used quantifies the inorganic phosphate liberated from phosphotyrosine after incubation with serum, followed by the deproteinization of the...
Jiayin Pang et al.
Physiologia plantarum, 154(4), 511-525 (2014-10-08)
The aim of this study was to investigate the capacity of three perennial legume species to access sources of varyingly soluble phosphorus (P) and their associated morphological and physiological adaptations. Two Australian native legumes with pasture potential (Cullen australasicum and...
Klaus Lorentz
Clinica chimica acta; international journal of clinical chemistry, 326(1-2), 69-80 (2002-11-06)
The continuous measurement of acid phosphatase (EC 3.1.3.2) activity in serum represents an analytical task not yet sufficiently accomplished. Introducing two novel substrates-2-chloro-4-nitrophenyl phosphate (CNP-P), which was preferred, and 4-nitronaphthyl-1-phosphate (NN-P)-an alternative assay to measure enzymatic activity was developed and...
Hongliang Tang et al.
Journal of plant physiology, 170(14), 1243-1250 (2013-06-12)
Acid phosphatases (APases) play a key role in phosphorus (P) acquisition and recycling in plants. White lupin (Lupinus albus L.) forms cluster roots (CRs) and produces large amounts of APases under P deficiency. However, the relationships between the activity of...
H G Drexler et al.
Leukemia, 8(3), 359-368 (1994-03-01)
Acid phosphatase (AcP, EC 3.1.3.2) is represented by a number of enzymes that can be differentiated according to structural and immunological properties, tissue distribution, subcellular location and other features; these AcP isoenzymes share similar catalytic activity toward phosphoesters in an...
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