• Journal of Plant Biology
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• v.21 no.1_4
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• pp.39-44
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• 1978

Acid phosphatase activities were analyzed in $\mu\textrm{g}$ tissue samples from an angiosperm parasite (Cuscuta cephalanthi) and its host plant (Hedera helix) by a fluorometric microtechnique. The apex and the coiling portion of the parasite axis exhibited greater enzyme activies than other portions of the hypha. Acid phosphatase activity in the haustorium was 2-3 times that in the hyphal axis. The vascular bundles of the normal host exhibited the greatest enzyme activity. The acid phosphatase activity in the host infected by the parasite decreased to the activity level of the haustorium.

• KSBB Journal
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• v.7 no.4
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• pp.302-307
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• 1992

Protein phosphatase 2A was obtained from a cytosolic fraction of bovine brain homogenate. The phosphatase activity using phosphorylated histone Hl as substrate was suppressed in the presence of liposomes composed of dipalmitoylphosphatidylcholine(DPPC) or the mixture of phosphatidylserine and DPPC. The binding of protein phosphatase to liposome was indicated by the facts that the phosphatase activity of the supernatant of protein phosphatase/multilayer vesicle mixture was decreased with increasing amount of liposome, and that [$^{125}I$]-labeled protein phosphatase was coeluted with liposome. However, the affinity of the protein for phospholipid membrane was not so high. On the other hand, okadaic acid and liposome reduced the phosphatase activity synergistically, which means that okadaic acid binds neither to lipid membrane nor to the membrane-associated phosphatase, The inhibitory effect of liposome was, therefore, ascribed to association of the protein phosphatase 2A with the lipid bilayer membrane.

• Biomedical Science Letters
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• v.5 no.1
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• pp.119-129
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• 1999

This study was aimed to investigate the enzyme-histochemical localization and characteristics of alkaline and acid phosphatase extracted from adult of Echinostoma hortense. Using the Gomori calcium stain and the Gomori lead nitrate satin method, we found that the alkaline and acid phosphatases were localized mostly in the intestine, vitellaria and pharynx of Echinostoma hortense. The three isozymes of alkaline phosphatase and two isozymes of acid phosphatase were separated from Echinostoma hortense by electrophoresis. The isozymes of alkaline phosphatase were 145.9, 207.5, 220.8 kDa and the isozymes of acid phosphatase were 179.5 and 209.4 kDa. The activity of alkaline phosphatase was denatured completely after heating at 9$0^{\circ}C$ for 12 seconds. The optimum pH and temperature for activity of alkaline phosphatase were about pH 9 and 4$0^{\circ}C$, while the optimum pH for activity of acid phosphatase was about pH 5. The maximum activity of alkaline phosphatase was at 189 unit, but maximum activity of acid phosphatase was at 71 unit As the result from above, we observed that alkaline and acid phosphatases funtion mainly in the alimentary tract and vitellaria. Echinostoma hortense performs the parasitism in the intestine of host by using proper isozyme of phosphatase.

• Parasites, Hosts and Diseases
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• v.31 no.2
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• pp.165-168
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• 1993

In order to know the enzyme activities of Filbricola seouzenis, an intestinal trematode of human and rodent in Korea. the enzyme histochemical method is applicated. Activities of acid phosphatase (E.C.3.1.3.2) and non-specific esterase (E.C.3.1.1) were present in microvilli and glandular cells of trlbocytic organ and the epithelium of the caecum.

• Korean Journal of Breeding Science
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• v.42 no.5
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• pp.455-462
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• 2010

Purple acid phosphatase is important for phosphorus remobilization in plants, but its role in plant adaptation to low phosphorus availability is not known. The cDNA encoding O. sativa purple acid phosphatase (OsPAP1) has 1008 bp with an open reading frame of 335 amino acid residues. The amino acid sequence of OsPAP1 cDNA shows of 50-51% identity with other plant purple acid phosphatases. OsPAP1 was expressed in rice plants and in cell cultures in the absence of phosphate ($P_i$). The expression was organ-specific with the strongest expression in $P_i$-deprived roots. Functional expression of the OsPAP1 gene in the transgenic Arabidopsis line was confirmed by northern and western blot analysis. OsPAP1 overexpression lines had higher phosphatase activity than wild-type. Overexpression of OsPAP1 in Arabidopsis plants resulted in increased Pi accumulation under Pi sufficient condition. These results show that the OsPAP1 gene represents more efficient $P_i$ uptake and can be used to develop new transgenic dicotyledonous plants.

• Korean Journal of Soil Science and Fertilizer
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• v.49 no.1
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• pp.44-52
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• 2016

Plants response to phosphate starvation include the changes of activity of some enzymes, such as phosphatases, fructose-1,6-bisphosphatase, sucrose-phosphate synthase and nitrate reductase. In this study, to determine the effects of phosphate starvation on the change of activities of acid and alkaline phosphatase, fructose-1,6-bisphosphatase, sucrose-phosphate synthase, and nitrate reductase were studied in melon seedlings (Cucumis melo L.). The content of the protein and chlorophyll tended to relatively reduced in melon seedlings subjected to phosphate starvation. Acid phosphatase activity in first and second leaves of melon seedlings was relatively higher than that of third and fourth leaves of seedlings in 14 days after phosphate starvation treatment, respectively. Active native-PAGE band patterns of acid phosphatase in melon leaves showed similar to activities of acid phosphatase, whereas alkaline phosphatase activity was different from the change in the activity of acid phosphatase. Inorganic phosphate content in melon seedlings leaves was constant. The changes of Fructose-1,6-bisphosphatase and sucrose phosphate synthase activities showed similar patterns in melon seedlings leaves, and between these enzymes activities and phosphate nutrition negatively related. Fructose-1,6- bisphosphatase and sucrose phosphate synthase activities showed significant difference in second and fourth leaves, but nitrate reductase showed significant difference in first and second leaves in 14days after phosphate starvation treatment. We concluded that phosphate nutrition could affect the distribution of phosphate, carbon and nitrogen in melon seedlings.

• Bulletin of the Korean Chemical Society
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• v.25 no.9
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• pp.1303-1304
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• 2004

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.490-495
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• 1994

Acid phosphatase (EC3.1.3.2) from carrots was partially purified by ammonium sulfate fractionation (30%-80%), Sephacryl S-200 gel filtration, cm-Sepharose CL-6B and DEAE -Sephacel ion exchange chromatography. The optimum ph and temperature of acid phosphatase from carrots were pH 5.5 and 55$^{\circ}C$, respectively. The enzyme was most stable at ph 6.0 and relatively unstable below pH 4.0 . The activation energy of the enayme was determined to be 10.6kcal/mole. The enzyme utilized p-nitrophenyl phosphate as a substrate among tested possible substrates, whereas it hydrolyzed 5' -IMP and 5'-GMP poorly. The Michaelis -Menten constant(Km) of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.55mM. Amongtested metal ions and inhibitors, Al+++ Zn++, Cu++ , fluoride, metavanadate and molybdate ions inhibited the enzyme activity drastically.

• Bulletin of the Korean Chemical Society
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• v.32 no.11
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• pp.4103-4105
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• 2011

• Applied Microscopy
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• v.3 no.1
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• pp.1-16
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• 1973

A combined cytochemical and electron microscopic study was carried out for the demonstration of acid phosphatase activities in trophozoites of E. histolytica. and E. gingivalis. E. histolytica(YS-27) strain was isolated from liver abscess of 72-year-old man in September 1969, and E. gingivalis (YS-215) strain was collected from gingival crevice of 41-year-old man in January 1972. The amoeba strains were maintained by subculture on diphasic medium, and used throughout the study. The results are summarized as follows; 1. In E. histolytica, the reaction products were distributed evenly over the entire surface of plasma membrane, whereas E. gingivalis showed no activity of acid phosphatase on the plasma membrane, except in the portion of the uroid-like structure. 2. In the cytoplasm, various reaction precipitates were observed in vacuoles of both amoebae; vacuole limiting membrane, vacuole membrane and its contents and lysosome-like structure. Strong enzyme active contents but membrane reaction negative vacuoles were conspicuous in E. gingivalis. Endoplasmic reticulum showed a moderate activity. 3. Granule-like acid phosphatase reaction product was demonstrated in the nucleoplasm of E. gingivalis, but it was negative in E. histolytica.