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Journal articles on the topic 'Acid phosphatase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Bialojan, C., and A. Takai. "Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics." Biochemical Journal 256, no. 1 (1988): 283–90. http://dx.doi.org/10.1042/bj2560283.

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The inhibitory effect of a marine-sponge toxin, okadaic acid, was examined on type 1, type 2A, type 2B and type 2C protein phosphatases as well as on a polycation-modulated (PCM) phosphatase. Of the protein phosphatases examined, the catalytic subunit of type 2A phosphatase from rabbit skeletal muscle was most potently inhibited. For the phosphorylated myosin light-chain (PMLC) phosphatase activity of the enzyme, the concentration of okadaic acid required to obtain 50% inhibition (ID50) was about 1 nM. The PMLC phosphatase activities of type 1 and PCM phosphatase were also strongly inhibited (

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2

Lorenc-Kubis, Irena. "Acid phosphatases in seeds and developing of squash (Cucurbita ficifolia)." Acta Societatis Botanicorum Poloniae 63, no. 1 (2014): 37–42. http://dx.doi.org/10.5586/asbp.1994.006.

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Changes in protein content and acid phosphatase activity were followed during germination (imbition through seedlings development) in extracts from cotyledons of squash (<i>Cucurbita ficifolia</i>). It has been shown that the activity of acid phosphatase was initially low and than increased to a maximum after 6 days of imbition. Acid phosphates were isolated from cotyledons of seeds and from 6-, 10- and 22-days old seedlings by extraction the proteins with 0.1 M acetate buffer pH 5.1, precipitation with ethanol and by affinity chromatography on con A-Sepharose. Two glycoprotein enz

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3

Takai, A., and G. Mieskes. "Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases." Biochemical Journal 275, no. 1 (1991): 233–39. http://dx.doi.org/10.1042/bj2750233.

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The phosphatase activities of type 2A, type 1 and type 2C protein phosphatase preparations were measured against p-nitrophenyl phosphate (pNPP), a commonly used substrate for alkaline phosphatases. Of the three types of phosphatase examined, the type 2A phosphatase exhibited an especially high pNPP phosphatase activity (119 +/- 8 mumol/min per mg of protein; n = 4). This activity was strongly inhibited by pico- to nano-molar concentrations of okadaic acid, a potent inhibitor of type 2A and type 1 protein phosphatases that has been shown to have no effect on alkaline phosphatases. The dose-inhi

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4

Jolivet, Pascale, Edith Bergeron, Haguith Benyair, and Jean-Claude Meunier. "Characterization of major protein phosphatases from selected species of Kluyveromyces. Comparison with protein phosphatases from Yarrowia lipolytica." Canadian Journal of Microbiology 47, no. 9 (2001): 861–70. http://dx.doi.org/10.1139/w01-081.

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Casein phosphatase activities have been identified in five yeast strains grown on Pi-deficient medium. Maximal endocellular activities appeared in the exponential phase. Exocellular phosphatases were significantly produced from Yarrowia lipolytica W-29 and Kluyveromyces marxianus, in the early stationary phase. Major phosphatases from K. marxianus were one heavy acid phosphatase composed of 6467 kDa subunits, which could be secreted in the medium, and one type 2A protein phosphatase with an apparent molecular mass of 147 kDa and a 52 kDa catalytic subunit dissociated by 80% ethanol treatment.

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5

Schiele, F., Y. Artur, A. Y. Floc'h, and G. Siest. "Total, tartrate-resistant, and tartrate-inhibited acid phosphatases in serum: biological variations and reference limits." Clinical Chemistry 34, no. 4 (1988): 685–90. http://dx.doi.org/10.1093/clinchem/34.4.685.

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Abstract We studied several factors affecting biological variation in serum acid phosphatases in a population of 1195 apparently healthy subjects four years old or older. We assayed total acid phosphatase activities in the presence of a transphosphorylating agent and using alpha-naphthyl phosphate as substrate. The main factors modifying total and tartrate-resistant acid phosphatases activities in serum are similar to those observed for total and bone alkaline phosphatases activities: age, sex, and hormonal state (puberty or menopause). The tartrate-inhibited acid phosphatase activity is, howe

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6

Gonzalez, Francisco, Antonio Vargas, Jose M. Arias, and Enrique Montoya. "Phosphatase activity during development cycle of Myxococcus xanthus." Canadian Journal of Microbiology 37, no. 1 (1991): 74–77. http://dx.doi.org/10.1139/m91-011.

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Cell-bound and extracellular acid and alkaline phosphatase activity have been studied in Myxococcus xanthus strains DK101, DK1050, DK2834, and DK2836. Both phosphatases were released into a liquid medium during vegetative growth and the levels were similar in all strains. On solid media, M. xanthus DK101 showed maximum activity at the end of the developmental process, when mature myxospores appeared. An increase in phosphatase activity was also observed in glycerol-induced myxospores. A transitory increase in phosphatase activity occurred during the germination of both glycerol-induced and fru

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7

Lundy, M. W., K. H. Lau, H. C. Blair, and D. J. Baylink. "Chick osteoblasts contain fluoride-sensitive acid phosphatase activity." Journal of Histochemistry & Cytochemistry 36, no. 9 (1988): 1175–80. http://dx.doi.org/10.1177/36.9.3403968.

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We used histological and biochemical methods to determine the cellular origin of bone matrix fluoride-sensitive acid phosphatase in chicken bone. Embryonic chicken calvariae were embedded in plastic and sections stained for acid phosphatase at various concentrations of substrate and fluoride. Acid phosphatase activity was observed in osteoblasts and osteoclasts but not in fibroblasts. Striking inhibition of osteoblastic acid phosphatase occurred at 100 microM fluoride, a concentration that had no apparent effect on osteoclastic acid phosphatase. Inhibition of osteoblastic and osteoclastic acid

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8

Nahas, E. "Control and localization of the phosphatases in conidia of Neurospora crassa." Canadian Journal of Microbiology 35, no. 9 (1989): 830–35. http://dx.doi.org/10.1139/m89-139.

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Repressible acid, repressible alkaline, and constitutive alkaline phosphatases were studied with respect to their control and localization in conidia of Neurospora crassa. In contrast to constitutive alkaline phosphatase, the production and secretion of repressible phosphatases is regulated by phosphate level and pH of the culture medium. Phosphatase activity increased with conidial germination and was detectable partially in the growth medium after 5 h incubation. These enzymes were found to be located in different cell compartments. Part of the whole cell enzyme activity involved a soluble e

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9

Chen, Xiaochi, Toshihiro Ansai, Shuji Awano, Toshiya Iida, Sailen Barik, and Tadamichi Takehara. "Isolation, Cloning, and Expression of an Acid Phosphatase Containing Phosphotyrosyl Phosphatase Activity fromPrevotella intermedia." Journal of Bacteriology 181, no. 22 (1999): 7107–14. http://dx.doi.org/10.1128/jb.181.22.7107-7114.1999.

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ABSTRACT A novel acid phosphatase containing phosphotyrosyl phosphatase (PTPase) activity, designated PiACP, from Prevotella intermedia ATCC 25611, an anaerobe implicated in progressive periodontal disease, has been purified and characterized. PiACP, a monomer with an apparent molecular mass of 30 kDa, did not require divalent metal cations for activity and was sensitive to orthovanadate but highly resistant to okadaic acid. The enzyme exhibited substantial activity against tyrosine phosphate-containing peptides derived from the epidermal growth factor receptor. On the basis of N-terminal and

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10

Hammond, K. D., R. K. Wollbrandt, and D. A. Gilbert. "Acid phosphatase and phosphoamino acid phosphatases in murine erythroleukaemic cells." International Journal of Biochemistry 17, no. 2 (1985): 259–64. http://dx.doi.org/10.1016/0020-711x(85)90124-7.

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11

Cotner Jr., James B., and Robert T. Heath. "Potential phosphate release from phosphomonoesters by acid phosphatase in a bog lake." Archiv für Hydrobiologie 111, no. 3 (1988): 329–38. http://dx.doi.org/10.1127/archiv-hydrobiol/111/1988/329.

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12

Pasqualini, S., F. Panara, and M. Antonielli. "Acid phosphatase activity in Pinus pinea – Tuber albidum ectomycorrhizal association." Canadian Journal of Botany 70, no. 7 (1992): 1377–83. http://dx.doi.org/10.1139/b92-173.

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Acid phosphatase activity of pine (Pinus pinea L.) roots was investigated in the presence or absence of the ectomycorrhizal fungus Tuber albidum Pico. Acid phosphatase activity was higher in mycorrhizal roots than in roots of uncolonized control plants. The optimum pH values for acid phosphatase were 3.5 and 5.0 for mycorrhizal roots and 5.0 for control roots. The acid phosphatase activity was inhibited by tartrate, fluoride, and molybdate ions, but a lower inhibition was exerted by orthophosphate. Mycorrhizal roots of pine possessed active acid phosphatases that hydrolyzed a wide variety of n

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13

Pasqualini, S., P. Batini, L. Ederli, F. Panara, and M. Antonielli. "Acid phosphatase isoforms in dry seeds and during seedling development in barley (Hordeum vulgare)." Canadian Journal of Botany 74, no. 5 (1996): 653–58. http://dx.doi.org/10.1139/b96-083.

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The acid phosphatase activity in the soluble, membrane, and cell wall fractions from Hordeum vulgare in dry seeds and during seedling development was investigated. The acid phosphatase activities were also assayed in barley roots and coleoptiles at different developmental stages. Electrophoretic patterns of multiple acid phosphatases in seeds, endosperms and embryos, and growing roots and coleoptiles are shown. The enzyme activity shows a rapid decrease in both roots and coleoptiles during growth. Using nondenaturing polyacrylamide gel electrophoresis, multiple acid phosphatase forms were foun

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14

Lorenc-Kubis, Irena, and Bronisław Morawiecka. "Phosphatase activity of Poa pratensis seeds. III. Effect of fluoride, citrate, urea and other substances on the activity of acid phosphatase Ia2 and Ia3." Acta Societatis Botanicorum Poloniae 47, no. 1–2 (2015): 83–89. http://dx.doi.org/10.5586/asbp.1978.007.

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Effects of fluoride, citrate, urea and other substances on the activity of acid phosphatase a<sub>2</sub> and a<sub>3</sub> toward p-nitrophenylphosphate and phenylphosphate were investigated. Both enzymes were inhibited by fluoride, p-chloromercuribenzoate and oxalate. Fluoride inhibited acid phosphatase a<sub>2</sub> noncorapetitively with p-mitrophenylphosphate, whereas acid phosphatase a<sub>3</sub> showed inhibition of mixed type. Hydrolysis of phenylphosphate by both acid phosphatases was activated by citrate. Cytosine and uridine inhibited

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15

Tsekova, Kolishka, Danka Galabova, and Kristina Todorova. "Copper Accumulation and Phosphatase Activities of Aspergillus and Rhizopus." Zeitschrift für Naturforschung C 55, no. 9-10 (2000): 708–12. http://dx.doi.org/10.1515/znc-2000-9-1007.

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Abstract Copper accumulation and phosphatase activities of three Aspergillus species resistant to copper were compared to three copper-sensitive Rhizopus species. High level of acid phosphatases and decreased Cu2+-uptake were found with resistant in contrast to sensitive strains. The presence of copper(II) ions in the medium increased the production of acid phosphatases in the resistant A. niger and decreased their activity in the sensitive R. delemar. Copper ions inhibited the activity of A. niger cellular acid phosphatase with a Ki of 8.9x10-4 ᴍ and slightly activated the R. delemar enzyme.

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16

Paulson, J. R., W. A. Ciesielski, B. R. Schram, and P. W. Mesner. "Okadaic acid induces dephosphorylation of histone H1 in metaphase-arrested HeLa cells." Journal of Cell Science 107, no. 1 (1994): 267–73. http://dx.doi.org/10.1242/jcs.107.1.267.

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It is shown here that treatment of metaphase-arrested HeLa cells with okadaic acid (0.15-2.5 microM) leads to dephosphorylation of histone H1. This effect is presumably due to the specific ability of okadaic acid to inhibit protein phosphatases 1 and/or 2A, because okadaic acid tetraacetate, which is not a phosphatase inhibitor, has no effect. Dephosphorylation of H1 does not occur if okadaic acid-treated cells are simultaneously treated with 20 nM calyculin A, or if the okadaic acid concentration is 5.0 microM or greater. The mechanism behind this phenomenon is not known. However, the results

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17

Hoopman, Todd C., Wei Wang, Chad A. Brautigam, Jennifer L. Sedillo, Thomas J. Reilly, and Eric J. Hansen. "Moraxella catarrhalis Synthesizes an Autotransporter That Is an Acid Phosphatase." Journal of Bacteriology 190, no. 4 (2007): 1459–72. http://dx.doi.org/10.1128/jb.01688-07.

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ABSTRACT Moraxella catarrhalis O35E was shown to synthesize a 105-kDa protein that has similarity to both acid phosphatases and autotransporters. The N-terminal portion of the M. catarrhalis acid phosphatase A (MapA) was most similar (the BLAST probability score was 10−10) to bacterial class A nonspecific acid phosphatases. The central region of the MapA protein had similarity to passenger domains of other autotransporter proteins, whereas the C-terminal portion of MapA resembled the translocation domain of conventional autotransporters. Cloning and expression of the M. catarrhalis mapA gene i

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18

Antibus, Robert K., Robert L. Sinsabaugh, and Arthur E. Linkins. "Phosphatase activities and phosphorus uptake from inositol phosphate by ectomycorrhizal fungi." Canadian Journal of Botany 70, no. 4 (1992): 794–801. http://dx.doi.org/10.1139/b92-101.

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To better understand the physiological importance of acid phosphatase activity we examined the effects of inorganic and organic phosphorus growth sources on enzyme activity and 32P uptake in several ectomycorrhizal fungi. Mycelium of eight isolates from four basidiomycete species demonstrated optimal p-nitrophenyl phosphatase activity at pH 4.5 or 5.0. Acid phosphatase activities varied between strains of Scleroderma citrinum and between the species examined. Interspecific differences in isozyme patterns of whole cell extracts were apparent in native polyacrylamide gels. The isoelectric points

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19

Rajvanshi, Indra, and K. L. Mali. "Biochemical and histochemical studies of alkaline and acid phosphatases in a digenetic trematode,Pegosomum egretti." Journal of Helminthology 60, no. 4 (1986): 293–98. http://dx.doi.org/10.1017/s0022149x00008518.

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ABSTRACTThe biochemistry and histochemistry ofPegosomum egrettihave been studied using standard techniques. Phosphatases were analysed colorimetrically; the optimum pH for acid phosphatase activity was 5·0 and for alkaline phosphatase was 10·0. The results were compared with those of other trematodes. Histochemical localization of acid and alkaline phosphatases revealed differences in enzyme activity in various tissues. These differences in the site and pattern of distribution of the two enzymes have been discussed in relation to transport of raw materials and the metabolism of the cell concer

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20

Paulson, J. R., J. S. Patzlaff, and A. J. Vallis. "Evidence that the endogenous histone H1 phosphatase in HeLa mitotic chromosomes is protein phosphatase 1, not protein phosphatase 2A." Journal of Cell Science 109, no. 6 (1996): 1437–47. http://dx.doi.org/10.1242/jcs.109.6.1437.

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Histone H1 is highly phosphorylated in mitotic HeLa cells, but is quickly dephosphorylated in vivo at the end of mitosis and in vitro following cell lysis. We show here that okadaic acid and microcystin-LR block the in vitro dephosphorylation of H1 and that they do so directly by inhibiting the histone H1 phosphatase rather than by some indirect mechanism. The concentrations of microcystin and okadaic acid required for inhibition strongly suggest that the histone H1 phosphatase is either PP1 or an unknown protein phosphatase with okadaic acid-sensitivity similar to PP1. The histone H1 phosphat

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21

Bize, Isabel, Patricia Muñoz, Mitzy Canessa, and Philip B. Dunham. "Stimulation of membrane serine-threonine phosphatase in erythrocytes by hydrogen peroxide and staurosporine." American Journal of Physiology-Cell Physiology 274, no. 2 (1998): C440—C446. http://dx.doi.org/10.1152/ajpcell.1998.274.2.c440.

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Indirect evidence has suggested that K-Cl cotransport in human and sheep erythrocytes is activated physiologically by a serine-threonine phosphatase. It is activated experimentally by H2O2and by staurosporine, a kinase inhibitor. Activation by H2O2and staurosporine is inhibited by serine-threonine phosphatase inhibitors, suggesting that the activators stimulate the phosphatase. The present study shows that sheep and human erythrocytes contain membrane-associated as well as cytosolic serine-threonine phosphatases, assayed from the dephosphorylation of32P-labeled glycogen phosphorylase. In cells

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22

Suter, Anke, Vincent Everts, Alan Boyde, et al. "Overlapping functions of lysosomal acid phosphatase (LAP) and tartrate-resistant acid phosphatase (Acp5) revealed by doubly deficient mice." Development 128, no. 23 (2001): 4899–910. http://dx.doi.org/10.1242/dev.128.23.4899.

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To date, two lysosomal acid phosphatases are known to be expressed in cells of the monocyte/phagocyte lineage: the ubiquitously expressed lysosomal acid phosphatase (LAP) and the tartrate-resistant acid phosphatase-type 5 (Acp5). Deficiency of either acid phosphatase results in relatively mild phenotypes, suggesting that these enzymes may be capable of mutual complementation. This prompted us to generate LAP/Acp5 doubly deficient mice. LAP/Acp5 doubly deficient mice are viable and fertile but display marked alterations in soft and mineralised tissues. They are characterised by a progressive he

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23

MacKintosh, C., and P. Cohen. "Identification of high levels of type 1 and type 2A protein phosphatases in higher plants." Biochemical Journal 262, no. 1 (1989): 335–39. http://dx.doi.org/10.1042/bj2620335.

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Extracts of Brassica napus (oilseed rape) seeds contain type 1 and type 2A protein phosphatases whose properties are indistinguishable from the corresponding enzymes in mammalian tissues. The type 1 activity dephosphorylated the beta-subunit of phosphorylase kinase selectively and was inhibited by the same concentrations of okadaic acid [IC50 (concentration causing 50% inhibition) approximately 10 nM], mammalian inhibitor 1 (IC50 = 0.6 nM) and mammalian inhibitor 2 (IC50 = 2.0 nM) as the rabbit muscle type 1 phosphatase. The plant type 2A activity dephosphorylated the alpha-subunit of phosphor

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24

Rao, A. V., K. Bala, and J. C. Tarafdar. "Dehydrogenase and phosphatase activities in soil as influenced by the growth of arid-land crops." Journal of Agricultural Science 115, no. 2 (1990): 221–25. http://dx.doi.org/10.1017/s0021859600075158.

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SUMMARYThe distribution of dehydrogenase activity (DHA) and the activities of phosphatases were studied in the rhizosphere of four varieties each of clusterbean (Cyamopsis tetragonoloba (L.) Taub.), mung bean (Vigna radiata (L.) Wilczek), moth bean (Vigna aconitifolia (Jacq.) Marechal) and pearl millet (Pennisetum americanum (L.) Leeke) grown in pots containing soil low in available P. Activities of dehydrogenase and phosphatases were greatest 25 days after sowing and remained constant from 50 days after sowing until crop maturity. Rhizosphere soils showed higher activities than other soils: 2

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Saleh, Mazen T., and John T. Belisle. "Secretion of an Acid Phosphatase (SapM) by Mycobacterium tuberculosis That Is Similar to Eukaryotic Acid Phosphatases." Journal of Bacteriology 182, no. 23 (2000): 6850–53. http://dx.doi.org/10.1128/jb.182.23.6850-6853.2000.

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ABSTRACT Mycobacterium tuberculosis secretes a large number of polypeptides with broad biological and immunological functions. We describe here the characterization of a 28-kDa acid phosphatase ofM. tuberculosis (SapM) localized to the culture filtrate. The mature protein demonstrated biochemical characteristics similar to those of the bacterial nonspecific acid phosphatases. However, SapM yielded significant sequence homology to fungal acid phosphatases and not those of bacteria. Thus, SapM may represent a new class of bacterial nonspecific acid phosphatases.

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Romas, Nicholas A., and Delbert J. Kwan. "PROSTATIC ACID PHOSPHATASE." Urologic Clinics of North America 20, no. 4 (1993): 581–88. http://dx.doi.org/10.1016/s0094-0143(21)00911-3.

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27

Caddick, Mark X., and Herbert N. Arst. "Structural genes for phosphatases inAspergillus nidulans." Genetical Research 47, no. 2 (1986): 83–91. http://dx.doi.org/10.1017/s0016672300022904.

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SUMMARYAlthough the fungusAspergillus nidulanshas a multiplicity of phosphatases and of genes where mutations affect one or more phosphatases, we have succeeded in identifying structural genes for three phosphatases as well as one other gene which might encode a fourth. Using both conditional and non-conditional mutations,palD has been shown to be the structural gene for a phosphate-repressible alkaline phosphatase,palG to be the structural gene for a non-repressible alkaline phosphatase which apparently exists in two electrophoretically distinct forms (but whose rates of thermal inactivation

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28

Valencia, Ana-Monstserrat, Jose Luis Oliva-Martinez, Guillermo Bodega, et al. "Identification of a protein-tyrosine phosphatase (SHP1) different from that associated with acid phosphatase in rat prostate." FEBS Lett 406, no. 1-2 (1997): 42–48. https://doi.org/10.1016/s0014-5793(97)00235-4.

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Using [32P]poly(Glu,Tyr) as substrate, we have identified, for the first time, in the rat prostatic gland a protein-tyrosine phosphatase activity different from that associated with prostatic acid phosphatase. Concanavalin A-Sepharose 4B was used to separate the two protein-tyrosyl phosphatases activities. The activity retained by the lectin had characteristics of the prostatic acid phosphatase. It was sensitive to inhibition by PNPP and the optimum pH shifted towards physiological values when [32P]poly(Glu,Tyr) was used as substrate. However, the major protein-tyrosine phosphatase activity wa

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29

Moorman, Veronica R., and Alexandra M. Brayton. "Identification of individual components of a commercial wheat germ acid phosphatase preparation." PLOS ONE 16, no. 3 (2021): e0248717. http://dx.doi.org/10.1371/journal.pone.0248717.

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Wheat germ acid phosphatase (WGAP) is a commercial preparation of partially purified protein commonly used in laboratory settings for non-specific enzymatic dephosphorylation. It is known that these preparations contain multiple phosphatase isozymes and are still relatively crude. This study therefore aimed to identify the protein components of a commercial preparation of wheat germ acid phosphatase using mass spectroscopy and comparative genomics. After one post-purchase purification step, the most prevalent fifteen proteins in the mixture included heat shock proteins, beta-amylases, glucoser

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30

Costa, Francilina Araujo, Joselita Cardoso de Souza, Josimara Nolasco Rondon, and Maria Catarina Megumi Kasuya. "Activity of Acid Phosphatases in Ectomycorrhizal Fungi." Journal of Agricultural Science 8, no. 3 (2016): 78. http://dx.doi.org/10.5539/jas.v8n3p78.

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<p>The colonization of plant roots by mycorrhizal fungi, generally increases P content in the host plant when in soils with low levels of P. The objective of this work was to evaluate the activity of acid phosphatases in two isolates of <em>Pisolithus microcarpus</em>, grown in different sources and concentrations of phosphate and to characterize the phosphatase isoenzymes produced by isolates. Both isolates were grown on Melin-Norkrans modified (MNM) medium enriched with organic (Po) or inorganic (Pi) sources of phosphorus, at five different concentrations, in order to study

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Caddick, Mark X., Alan G. Brownlee, and Herbert N. Arst. "Phosphatase regulation inAspergillus nidulans: responses to nutritional starvation." Genetical Research 47, no. 2 (1986): 93–102. http://dx.doi.org/10.1017/s0016672300022916.

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SUMMARYThe regulation of the syntheses of a number of phosphatases in the fungusAspergillus nidulanshas been examined. Levels of the intracellular alkaline phosphatase P11 are increased by starvation for carbon, nitrogen, phosphorus or sulphur. There is, however, no evidence that any of the wide domain regulatory genes which mediate sufficiency-triggered repression for each of these elements involved. A possible interpretation is that all four forms of starvation result in accumulation of an inducing metabolite. ThepalcA gene has been identified as a wide domain, probably positive-acting regul

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Whitaker, K. B., T. M. Cox, and D. W. Moss. "An immunoassay of human band 5 ("tartrate-resistant") acid phosphatase that involves the use of anti-porcine uteroferrin antibodies." Clinical Chemistry 35, no. 1 (1989): 86–89. http://dx.doi.org/10.1093/clinchem/35.1.86.

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Abstract We describe an immunoassay for human band-5 acid phosphatase in which antibodies to porcine uteroferrin, immobilized on Sepharose particles, are used. Band-5 acid phosphatase is the tartrate-resistant isoenzyme normally expressed in tissue macrophages such as osteoclasts and alveolar macrophages. The immunoassay is similar in reproducibility and sensitivity to assays based on inhibition by d-tartrate. However, compared with the latter, the greater specificity of the immunoassay makes it markedly less susceptible to errors arising from the presence of non-band-5 acid phosphatases, e.g.

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33

Wyss, Markus, Luis Pasamontes, Roland Rémy, et al. "Comparison of the Thermostability Properties of Three Acid Phosphatases from Molds: Aspergillus fumigatusPhytase, A. niger Phytase, and A. nigerpH 2.5 Acid Phosphatase." Applied and Environmental Microbiology 64, no. 11 (1998): 4446–51. http://dx.doi.org/10.1128/aem.64.11.4446-4451.1998.

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ABSTRACT Enzymes that are used as animal feed supplements should be able to withstand temperatures of 60 to 90°C, which may be reached during the feed pelleting process. The thermostability properties of three histidine acid phosphatases, Aspergillus fumigatus phytase,Aspergillus niger phytase, and A. niger optimum pH 2.5 acid phosphatase, were investigated by measuring circular dichroism, fluorescence, and enzymatic activity. The phytases ofA. fumigatus and A. niger were both denatured at temperatures between 50 and 70°C. After heat denaturation at temperatures up to 90°C, A. fumigatus phytas

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34

Paradis, Gilles, Jean Y. Dubé, Pierre Chapdelaine, and Roland R. Tremblay. "In vitro translation of human prostatic acid phosphatase mRNA and processing of the translation products by microsomal membranes and endoglycosidase H." Biochemistry and Cell Biology 65, no. 10 (1987): 921–24. http://dx.doi.org/10.1139/o87-119.

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Poly(A)+ RNA was isolated from human prostatic tissue and translated in vitro in a rabbit reticulocyte lysate translation assay. Acid phosphatase labeled with [35S]methionine was immunoprecipitated with an antibody against seminal plasma acid phosphatase. Two-dimensional polyacrylamide gel electrophoresis of the immunoprecipitate, followed by fluorography, revealed the presence of two spots (one major and one minor), both having a molecular mass of 43 kilodaltons (kDa) and an isoelectric point higher than mature acid phosphatase. Addition of canine pancreatic membranes to the translation assay

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35

MacKintosh, C., J. Coggins, and P. Cohen. "Plant protein phosphatases. Subcellular distribution, detection of protein phosphatase 2C and identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase." Biochemical Journal 273, no. 3 (1991): 733–38. http://dx.doi.org/10.1042/bj2730733.

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Protein phosphatases 1 and 2A (PP1 and PP2A) were identified in a variety of plant cells and found to be particulate or soluble depending on the species. In extracts prepared from oilseed-rape seeds these enzymes were associated with microsomes and more rapidly sedimenting fractions, whereas in wheat leaf extracts they were largely microsomal, the remainder being present in the soluble fraction. In pea leaf and carrot cell extracts PP1 and PP2A were almost entirely soluble. No PP1 or PP2A activity was associated with the membranes or stroma of chloroplasts in oilseed-rape seeds, pea leaves and

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36

Yi, T. L., J. L. Cleveland, and J. N. Ihle. "Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13." Molecular and Cellular Biology 12, no. 2 (1992): 836–46. http://dx.doi.org/10.1128/mcb.12.2.836-846.1992.

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Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We a

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Yi, T. L., J. L. Cleveland, and J. N. Ihle. "Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13." Molecular and Cellular Biology 12, no. 2 (1992): 836–46. http://dx.doi.org/10.1128/mcb.12.2.836.

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Abstract:

Protein tyrosine phosphorylation has been implicated in the growth and functional responses of hematopoietic cells. Recently, approaches have been developed to characterize the protein tyrosine phosphatases that may contribute to regulation of protein tyrosine phosphorylation. One novel protein tyrosine phosphatase was expressed predominantly in hematopoietic cells. Hematopoietic cell phosphatase encodes a 68-kDa protein that contains a single phosphatase conserved domain. Unlike other known protein tyrosine phosphatases, hematopoietic cell phosphatase contains two src homology 2 domains. We a

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38

Knypl, J. S. "Molecular forms of phosphatase and ribonuclease in phosphate deficient and N,N-dimethylmorpholinium chloride treated Spirodela oligorrhiza (Lemnaceae)." Acta Societatis Botanicorum Poloniae 48, no. 1 (2015): 65–85. http://dx.doi.org/10.5586/asbp.1979.006.

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Soluble, membrane bound, and extracellular phosphatases (EC 3.1.3.2 and 3.1.3.1) of control, N,N-dimethylmorphołinłum chloride (DMMC) treated, and phosphate deficient (-P) axenic <i>Spirodela oligorrhiza</i> plants were analysed by Sephadex G-150 gel filtration. Soluble, acid enzymes of control plants were separated into two molecular forms with apparent MW ≥ 400 000 and 85 000. Phosphatase with MW 34 000 replaced the latter isoenzyme in the presence of DMMC. Two alkaline enzymes with apparent MW 210 000 and 36 000 were detected in -P plants. Triton X-100 solubilized a number of ac

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Kong, Hoon-Young, Hak-Jong Lee, and Jong-Hoe Byun. "Roles of Prostatic Acid Phosphatase in Prostate Cancer." Journal of Life Science 21, no. 6 (2011): 893–900. http://dx.doi.org/10.5352/jls.2011.21.6.893.

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Passos Lemos, Adriana dos, André Luís Fonseca de Souza, Ana Acacia de Sá Pinheiro, Márcia de Berrêdo-Pinho, and José Roberto Meyer-Fernandes. "Ecto-phosphatase Activity on the Cell Surface of Crithidia deanei." Zeitschrift für Naturforschung C 57, no. 5-6 (2002): 500–505. http://dx.doi.org/10.1515/znc-2002-5-617.

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In the present work we have partially characterized an ecto-phosphatase activity in Crithidia deanei, using viable parasites. This enzyme hydrolyzed p-nitrophenylphosphate at a rate of 3.55 ± 0.47 nmol Pi/h x 108 cells. The dependence on p-NPP concentration shows a normal Michaelis-Menten kinetics for this phosphatase activity and the value of the apparent Km for p-NPP was 5.35 ± 0.89 mᴍ. This phosphatase activity was inhibited by the product of the reaction, the inorganic phosphate. Experiments using classical inhibitors of acid phosphatases, such as ZnCl2 and sodiumfluoride , as well as inhi

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Roiko, Katja, Olli A. Jänne, and Pirkko Vihko. "Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases." Gene 89, no. 2 (1990): 223–29. http://dx.doi.org/10.1016/0378-1119(90)90009-g.

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42

Aumüller, Gerhard, Helmut Vedder, Ulrike Enderle-Schmitt, and Jürgen Seitz. "Cytochemistry and biochemistry of acid phosphatases VII: Immunohistochemistry of canine prostatic acid phosphatase." Prostate 11, no. 1 (1987): 1–15. http://dx.doi.org/10.1002/pros.2990110102.

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43

Cottrill, Michael A., Serguei P. Golovan, John P. Phillips, and Cecil W. Forsberg. "Inositol phosphatase activity of theEscherichia coli agp-encoded acid glucose-1-phosphatase." Canadian Journal of Microbiology 48, no. 9 (2002): 801–9. http://dx.doi.org/10.1139/w02-076.

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When screening an Escherichia coli gene library for myo-inositol hexakisphosphate (InsP6) phosphatases (phytases), we discovered that the agp-encoded acid glucose-1-phosphatase also possesses this activity. Purified Agp hydrolyzes glucose-1-phosphate, p-nitrophenyl phosphate, and InsP6with pH optima, 6.5, 3.5, and 4.5, respectively, and was stable when incubated at pH values ranging from 3 to 10. Glucose-1-phosphate was hydrolyzed most efficiently at 55°C, while InsP6and p-nitrophenyl phosphate were hydrolyzed maximally at 60°C. The Agp exhibited Kmvalues of 0.39 mM, 13 mM, and 0.54 mM for the

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du Plessis, Erika, Jacques Theron, Eldie Berger, and Maureen Louw. "Evaluation of the Staphylococcus aureus Class C Nonspecific Acid Phosphatase (SapS) as a Reporter for Gene Expression and Protein Secretion in Gram-Negative and Gram-Positive Bacteria." Applied and Environmental Microbiology 73, no. 22 (2007): 7232–39. http://dx.doi.org/10.1128/aem.01030-07.

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ABSTRACTA phosphatase secreted byStaphylococcus aureusstrain 154 has previously been characterized and classified as a new member of the bacterial class C family of nonspecific acid phosphatases. As the acid phosphatase activity can be easily detected with a cost-effective plate screen assay, quantitatively measured by a simple enzyme assay, and detected by zymography, its potential use as a reporter system was investigated. TheS. aureusacid phosphatase (sapS) gene has been cloned and expressed from its own regulatory sequences inEscherichia coli,Bacillus subtilis, andBacillus halodurans. Tran

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Santric, Ljiljana, Ljiljana Radivojevic, Slavica Gasic, Radmila Stankovic-Kalezic, and Jelena Gajic-Umiljendic. "Effects of metribuzin on the activity of some enzymes in soil." Pesticidi i fitomedicina 23, no. 3 (2008): 189–94. http://dx.doi.org/10.2298/pif0803189s.

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Effects of metribuzin on the activity of some enzymes in soil was investigated. Trials were set up in the laboratory on a clay loam soil. Metribuzin was applied at 12.0, 24.0 and 60.0 mg/kg soil rates and soil samples were collected 3, 7, 15, 30 and 45 days after metribuzin treatment for analyses. Alkaline phosphatase, acid phosphatase, dehydrogenase, urease and ?-glucosidase were recorded. The results showed that the intensity of metribuzin effects on the activity of enzymes depended on treatment rate, exposure time and enzyme group. Metribuzin had an inhibiting effect on acid phosphatese and

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Lorenc-Kubis, I., B. Morawiecka, M. Niezgódka, and A. Hebrowska. "Phosphatase activity of Poa pratensis seeds. II. Purification and characterization of acid phosphatase Ia2 and Ia3." Acta Societatis Botanicorum Poloniae 44, no. 2 (2015): 255–63. http://dx.doi.org/10.5586/asbp.1975.022.

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Two acid phosphatases (Ia2, Ia3) have been isolated from <i>Poa pratensis</i> seeds and partially purified. Both enzymes showed maximal activity at pH 4,9. They exhibited high activity towards p-nitrophenyl phosphate, inorganic pyrophosphate and phenyl phosphate, much less activity towards glucose-6 phosphate, and mononucleotides. Phosphatases a<sub>2</sub> and a<sub>3</sub> differed in their activity towards ADP. Orthophosphate, fluoride and Zn<sup>2+</sup> were effective inhibitors. EDTA, β-mercaptoethanol and Mg<sup>2+</sup> activa

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Southey, M. C., D. M. Findlay, and B. E. Kemp. "Regulation of membrane-associated tyrosine phosphatases in UMR 106.06 osteoblast-like cells." Biochemical Journal 305, no. 2 (1995): 485–90. http://dx.doi.org/10.1042/bj3050485.

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Protein tyrosine phosphatases play an important role in cell metabolism. Three distinct protein tyrosine phosphatase activities have been identified in an osteoblast-like cell line, UMR 106.06. These activities comprised two membrane-associated phosphatases and one cytosolic phosphatase of apparent molecular mass > 153 kDa, 80 kDa and 40 kDa respectively, estimated by gel filtration. On the basis of differences in apparent molecular mass, proteolytic-digestion profiles, substrate specificities and responses to a range of extracellular influences and inhibitor molecules, the two membrane-ass

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Vihko, P. "Prostatic Acid Phosphatase (PAP)." Scandinavian Journal of Clinical and Laboratory Investigation 48 (1988): 47–48. http://dx.doi.org/10.3109/00365518809168500.

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AKUZAWA, Ryozo, and Patrick F. FOX. "Acid phosphatase in cheese." Animal Science Journal 75, no. 5 (2004): 385–91. http://dx.doi.org/10.1111/j.1740-0929.2004.00202.x.

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Vihko, P. "Prostatic Acid Phosphatase (PAP)." Scandinavian Journal of Clinical and Laboratory Investigation 48, sup190 (1988): 47–48. http://dx.doi.org/10.1080/00365518809168500.

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