• 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.

• 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.

• Archives of Pharmacal Research
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• v.22 no.5
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• pp.464-473
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• 1999

Regulation of phosphcholine-hydrolyzing phosphatase (phosphocholine-phosphatase) activity, purified from bovine brain, was examined under physiological conditions. Various endogenous phosphomonoesters, which were utilized as substrate, inhibited the phosphocoline-phosphatase activity competitively (Ki 5.5-$82.0 {\mu}M$); among phosphomonoesters tested, there was a similar order of capability between the binding affinity of substrate and the inhibitory potency. In addition, phosphate ions also inhibited the phosphatase activity competitively with a Ki value of approximately $16{\mu}M$. Although leucine or theophylline inhibited the phosphatase activity at pH 9.0, their inhibitory action decreased greatly at pH 7.4. The pH-Km and pH-Vm profiles indicate that ionizable amino acids are involved in substrate binding as well as catalysis, alluding that the phosphatase activity may be highly dependent on the intracellular pH. Amino acid modification study supports the existence of tyrosine, arginine or lysine residue in the active site, and the participation of tyrosine residue in the catalytic action may e suggested positively for the susceptibility to the action of tetranitromethane or HOl-generator. Separately, the oxidative inactivation of phosphocholine-phosphatase activity was investigated. Of oxidants tested, HOONO, HOCl, HOl and $ascorbate/Cu^{2+}$ system were effective to inactivate the phosphatase activity. Noteworthy, a remarkable inativation was accomplished by $30{\mu}M$ HOCl in combination with 1 mM Kl. Inaddition, $Cu^{2+}(3{\mu}M) $in combination with ascorbate at concentrations as low as 0.1-0.3 mM reduced the phosphatase activity to a great extent. From these results, it is proposed that the phosphocholine-phosphatase activity may be regulated endogenously and susceptible to the various oxidant system in vivo.

• 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.

• 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.

• 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).

• The Korean Journal of Zoology
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• v.17 no.4
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• pp.177-184
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• 1974

The cobalt capture method of Gomori's modified technique(Gomori, 1952) was employed to study the histochemistry of the developing frog kidney. Alkaline phosphatase activity was observed in association with the brush borders of pronephros and mesonephros. By the stage of transition from larva to tadpole alkaline phosphatase activity was gradually increased in the brush border of pronephros, and as the pronephros begun to degenerate the enzyme activity was decreased and disappeared. By the time of maximum development of the pronephros the mesonephros began to develop and alkaline phosphatase activity of the mesonephric tubules showed highly positive throughout the stage of metamorphosis. No activity was observed in association with the collecting tubules and ductal elements.

• Journal of Microbiology
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• v.33 no.4
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• pp.267-272
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• 1995

Phosphatase activity was measured with other environmental factors in Cheonho reservoir in 1994. It ranged form 95 to 1,685 nM/1/h and was correlated significantly with chlorophyll-a. Such a close relation well matched the fact that over 90% of phosphatase activity was detected in > 3 $\mu\textrm{m}$ fraction. The phosphatase activity also correlated negatively with dissolved inorganic phosphate concentration, which implies derepression of phosphatase production by phosphate limitation. Significant correlation was analyzed between phosphatase activity and BOD, which also appeared to be closely correlated with chlorophyll-a. A great percentage of organic materials seems to be generated autochthonously by algae and extracellular enzyme even though allochthonous influence was thought to be stronger in Cheonho reservoir.

• 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 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.