• Journal of Environmental Health Sciences
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• v.17 no.2
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• pp.121-126
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• 1991

To clarify a cause of increased serum level of acid phosphatase in CCl$_{4}$-treated rats, the acid phosphatase activity of liver was compared with that serum. Concomitantly, the serum and liver acid phosphatase activity of CCl$_{4}$-treated rats were compared with that of CCl$_{4}$-treated rats pretreated with prednisolone or actinomycin D. In CCl$_{4}$-treated rats, the activity of serum acid phosphatase was significiantly increased whereas that of liver acid phosphatase was rather slightly decreased. the pretreatment of prednisolone led to the decreased activity of serum and liver acid phosphatase in CCl$_{4}$-treated rats. But the pretreatment of actinomycin D rather increased the activity of liver and serum enzyme. In conclusion, it is likely the increased activity of serum acid phosphatase is based on the excess leaking of acid phosphatase into blood by the increased membrane permeability of both liver cell and lysosome in it.

• Journal of Plant Biotechnology
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• v.29 no.4
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• pp.277-280
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• 2002

Acid phosphatase in the radish young plant showed optimal activity at pH 5.5. The activity of acid phosphatase was maintained longer during the ABA (0.5 mM) treatment than those in control, whereas that was similar to the treatment of NaCl (0.5 mM). But during the cold (4$^{\circ}C$) treatment, the activity of acid phosphatase was decreased dramatically compared to the control, which was maintained almost on a constant level and increased gradually during 6 days. It showed that acid phosphatase was in relation to the change of biochemical reaction, which plants were coped with cold, NaCl and ABA stress.

• 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.

• 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.

• Biomedical Science Letters
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• v.10 no.4
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• pp.429-434
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• 2004

The effects of intravenous administration of high concentration of taurocholic acid (TCA) on cathepsin B and D, and acid phosphatase activities in rat liver lysosome were studied. These liver lysosomal enzymes were determined from the experimental rats with choledocho-caval shunt (CCS). The activities of liver lysosomal cathepsin B and D, and acid phosphatase were found to be significantly increased in the CCS plus TCA injection group than in control group, such as group of CCS alone group. However, these hepatic enzyme activities did not change in the CCS plus tauroursodeoxycholic acid injection group. The above results suggest that TCA stimulates the biosynthesis of the lysosomal cathepsin B and D, and acid phosphatase in the liver.

• The Korean Journal of Zoology
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• v.16 no.2
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• pp.139-145
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• 1973

The activity of acid and alkaline phosphatases of pine moth, Dendrolimus spect abilis Butler was measured in a serier of developmental stages ranging from the larva to the adult. The activity of both enzymes increased gradually with age of larvae, and then decreased in the prepupal stage. Acid enzyme was at a maximum in the pupal early stage and alkaline enzyme in the 8th instar larva, respectively. And in the prepupal stage there were no significant differences between both acid and alkalnie phosphatases. However, their activities were far lower than in the 8th instar larva. In the pupal early stage there occurs a increase in the acitivity of acid enzyme followed by a decrease in the pupal later stage, and in the adult stage its activity increased again.

• Microbiology and Biotechnology Letters
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• v.13 no.4
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• pp.403-408
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• 1985

Enhancement of surfactant on release of secretory enzyme, such as $\alpha$-amylase, acid phosphatase and alkaline phosphatase, was investigated during submerged culture of Rhizopus oryzae. Morphological changes of colony was occured; small pelletal form in 0.18mM of sodium dodecyl sulfate, pulpy form in 0.48mM of sodium deoxycholate, and filamentous form in absence of surfactant. It. Supplement of sodium dodecyl sulfate induced 9 times increasing activity of $\alpha$-amylase and that of acid phosphatase 25 times in cultural fluids. Alkaline phosphatase was increased 11 times in cultural fluid and also stimulated in cytoplasm with supplement of sodium deoxycholate.

• Journal of Life Science
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• v.11 no.5
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• pp.489-495
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• 2001

The effect of ozone-water treatment on the morphological change of endosperm cells and the activity of acid phosphatase during Glycine max germination was investigated with electron microscope. Acid phosphatase showed the activity in the cell organelles of germinating endosperm of seed. it's activity occurrs in 12 hrs cultivation after 0.5 ppm ozone-water treatment. As the differentiation of endosperm, reaction products of the acid phosphatase appear to be accumulated invacuole after treatment of ozone-water. This result confirm that acid phosphatase is inveolved in the decomposition and translation of the intracellular storage materials. The characteristics of grganelle in the endosperm cell during germination were discussed.

• 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.