• 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.

• 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.

• Applied Biological Chemistry
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• v.38 no.5
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• pp.376-381
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• 1995

Thermus caldophilus GK24 was selected as sources of thermostable alkaline phosphatase from a survey of extreme thermophile. T. caldophilus GK24 was tested for production of alkaline phosphatase by addition of various concentration of sodium glutamate, bactotryptone, glucose and yeast extract to basal salts. Sodium glutamate was found to be effective for the alkaline phosphatase induction. The optimal induction medium for production of alkaline phosphatase involves the addition of 0.3% sodium glutamate, 0.2% bactotryptone and 0.5% glucose to basal salts. The activity of the enzyme in optimal induction medium increased nearly 6-fold/ml than basal medium and 27.5-fold/ml than standard medium. T. caldophilus GK24 alkaline phosphatase was found to be inducible. When starved of inorganic phosphate, T. caldophilus GK24 produces the enzyme alkaline phosphatase. The addition of inorganic phosphate to growth medium had a repressive effect on enzyme synthesis.

• 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.

• The Korean Journal of Zoology
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• v.17 no.4
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• pp.167-176
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• 1974

The authors have studied the distribution of alkaline phosphatase in the pharynx, esophagus, stomach (or intestinal bulb), anterior and posterior portions of intestine of three kinds of fishes. The results obtained are as follows: 1. Alkaline phosphatase activity of basal cells in the pharyngeal epithelium of loach and snakehead fish showed moderately positive reaction, and basal cells in the esophagel epithelium of loach and eel showed also moderately positive reaction. 2. Goblet cells of pharynx, esophagus, intestinal bulb and intestinal mucosa, and gastric glandular cells of the above fishes showed negative reaction for alkaline phosphatase. 3. Strongly positive reaction for alkaline phosphatase was observed at both intestinal bulb and the free border of intestinal epithelium, but weak positive reaction at the free border of posterior portion of loach intestine.

• 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.

• Clinical and Experimental Reproductive Medicine
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• v.8 no.2
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• pp.1-11
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• 1981

The quantitative analyses of the phosphatase activity in the endometrium of the rat ovariectomized on Day 2 of pregnancy was carried out in comparison with the intact one, in order to investigate the hormonal dependency of the uterus prior to the implantation, and to study the phosphatase activity in the endometrial tissues in vitro incubated in different acidity of the medium. The results obtained were as follows: 1. The activity of the total phosphatase was the highest at Day 3 of pregnancy of the intact animals irrespective of acidity of the medium. However, the ovariectomized rat showed its peak somewhat delayed. The time of the highest activity of the enzymes was matched with the time of high secretion of the ovarian hormones. 2. The activity of acid phosphatase in the endometrium was twice or four times as much high as that of neutral or alkaline phosphatase, respectively. 3. The activity of alkaline phosphatase was rather steady in Day 3 through Day 5 of the pregnancy of the rat intact or ovariectomized but with low level compared to those of other phosphatase. 4. The present re~lt indicated more important role by $Mg^{2+}$-dependent phosphatase than by $K^+$-dependent one for the preparation for decidualization.

• The Journal of the Korean dental association
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• v.13 no.6
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• pp.529-531
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• 1975

This observation was carried out to investigate the phosphatase activity and the calcium contents of periapical granuloma in patients of both sex and different age. The results were as follows : 1. Acid phosphatase activity was considerably increased with bone absorption. 2. Alkaline phosphatase activity was also remarkably increased in periapical granuloma. 3. In case of periapical granuloma, differences of phosphatase activity by age and sex were not observed. 4. Calcium contents in periapical granuloma was of very small quantity, showing remarkable decrease when compared with the normal bone tissue.

• Korean Journal of Clinical Pharmacy
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• v.9 no.1
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• pp.62-65
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• 1999

Inorganic phosphate (Pi) in rabbit plasma was found to block completely phosphotyrosine phosphatase (PTPase) activity without affecting the alkaline phosphatase (ALPase) activity. Our results provided that (1) PTPase activity and inhibitor are separated after G-25 gel-filtration. (2) This inhibitor is heat stable and trypsin-resistant and it can be removed by dialysis using 3 Kd cut-off tubing. (3) The elution pattern of the inhibitor is identical to that of Pi, and by performing a seperate run with inorganic phosphate. (4) The PTPase activity was recovered following an incubation with $CaCl_2$ (10 mM).