• Journal of Plant Biology
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• v.21 no.1_4
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• pp.13-21
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• 1978

The effect of cyclic-AMP on the induction of acid phosphatase activity in barley aleurone layers was examined. Tannic acid was used as a inhibitor. Decursinol and coumarin were also used as a comparison. Maxiumu promotion of the enzyme activity was obtained with 10-5M cyclic-AMP, but this promotion was lower than that of 10-5M GAS induced enzyme activity in incubation medium. The inhibition rate in the addition of tannic acid was shown 17% and 63% at a ratio to GAs (by weight) of 10 : 1, and 58% and 94% at a ratio of 100 : 1 treated with GAs, and cyclic-AMP, respectively. The most potentiation of 10-6M GAS effect was induced by the additiion of suboptimal concentration (10-6M) of cyclic-AMP. Additional GAs and cyclic-AMP were shown the recovery of the enzyme activity inhibited by tannic acid. The combination with cyclic-AMP and theophylline enhanced the enzyme activity, too. Any other nucleotides tested except cyclic-AMP didn't show the action. There were no differences in acid phosphatase isozyme patterns by polyacrylamide disc electrophoresis, in conjunction with the different additions but the size of bands showed great differences. Especially, the 3rd band and the 5th band group were remarkable.

• Journal of Periodontal and Implant Science
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• v.4 no.1
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• pp.12.2-12.2
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• 1974

• The Korean Journal of Ecology
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• v.14 no.1
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• pp.101-111
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• 1991

Amoeba sp. was cultured under the light and the dark conditions, and the activity of phosphatases was investigated. There was a linear correlation between the early reaction time and the activity of phosphatases when phosphatases were incubated at 30℃. Then the activity of acid phosphatase was about 2 times higher than that of alkaline phosphatase. The activity of phosphatase was optimal at pH 5.0 in acidic part and at pH 8.0 in alkaline part, respectively. The optimal temperature of phosphatases was near the 40℃. The isozyme patterns of cytoplasmic acid phosphatase were compared with those of membraneous one. Both the isozyme patterns were shown to bo polymorphic on the polyacyamide gel, but different band patterns were observed in the isozymes of the cytoplasmic and the membraneous acid phosphatases. The number of Amoeba sp. under the light stimulus for 48 hours decreased negative exponentially from the illumination. The activity of acid and alkaline phosphatases under the illumination of light incresed 1.7 and 1.5 times higher, respectively, than the activity of those under the dark condition. This result apperars to be related to the mechanism of the autophosphorylation.

• Journal of Sericultural and Entomological Science
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• v.21 no.1
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• pp.21-28
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• 1979

The Electrophoretic separation in agarose gel on the esterase and acid phosphatase of blood, midgut and silk gland was carried out with 2 original variginal varieties and 7 F$_1$ hybrids. 1. The midgut of larvae fed on mulberry leaves showed one or two more esterase bands than that of larvae fed on artificial diet. 2. The midgut of C 15 larvae being excellently respondent to artificial diet showed one or two more esterase bands than that of larvae being bad respondent to artificial diet. 3. Electrophoretic separation of esterase bands appeared to be greatly different among newly hatched larvae, 1st and 2nd install larvae of F$_1$hybrids. However the difference among the silkworm varieties was not recognized. 4. According to the change in rearing temperature, the number of the active band of midgut esterase was varied. At the temperature of 28$^{\circ}C$ 5 active esterase bands were found. At temperature of 35$^{\circ}C$ 4 bands were noted at 3rd install and 6 or 7 bands at 4th instar. 5. No similar esterase bands conld be found among midgut, blood and silkgland. There are five esterase bands in the midgut, one in blood and three in silkgland. 6. There was rather small difference in acid phosphatase types of midgut and blood according to varieties and rearing temperature. No active band was shown in silkgland. In midgut, there was one acid phosphatase band at 3rd install, two at 4th instar and three at 5th instar. In blood, One active band at 3rd or 4th instar and three bands at 5th inatar were detected.

• Journal of Periodontal and Implant Science
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• v.17 no.1
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• pp.109.2-109.2
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• 1987

• Bulletin of the Korean Chemical Society
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• v.32 no.1
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• pp.31-32
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• 2011

• Journal of Food Hygiene and Safety
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• v.9 no.2
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• pp.75-80
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• 1994

The effects of ursodeoxycholic acid (UDCA) were studied on the hepatotoxicity induced by several hepatotoxicants such as carbonte trachloride, thioacetamide and 1-naphthylisothiocyanate in ICR male mice. UDCA (50 mg/kg, 100 mg/kg) decreased the elevated serum bilirubin in carbon tetrachloride intoxicated mice, the elevated serum AST, alkaline phosphatase in thioacetamide intoxicated mice, the elevated serum AST and bilirubin in 1-naphthylisothiocyanate intoxicated mice.

• Journal of Life Science
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• v.21 no.6
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• pp.893-900
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• 2011

Prostatic acid phosphatase (PAP) is one of the widely used biomarkers in the diagnosis of prostate cancer. It was initially identified in 1935 and is the most abundant phosphatase in the human prostate. PAP is a prostate-specific enzyme that is synthesized in prostate epithelial cells. It belongs to the acid phosphatase group that shows enzymatic activity in acidic conditions. PAP is abundant in prostatic fluid and is thought to have a role in fertilization and oligospermia. It also has a potential role in reducing chronic pain. But one of the most apparent functions of PAP is the dephosphorylation of macromolecules such as HER-2 and PI3P that are involved in the ERK1/2 and MAPK pathways, which in turn leads to inhibition of cell growth and tumorigenesis. Currently, clinical trials using PAP DNA vaccine are underway and FDA-approved immunotherapy using PAP is commercially available. Despite these clinically important aspects, molecular mechanisms underlying PAP regulation are not fully understood. The promoter region of PAP was reported to be regulated by NF-${\kappa}B$, TNF-${\alpha}$, IL-1, androgen and androgen receptors. Here, the features of PAP gene and protein structures together with the function, regulation and roles of PAP in prostate cancer are discussed.

• Parasites, Hosts and Diseases
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• v.31 no.4
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• pp.353-362
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• 1993

The present study was carried out to investigate the localization and isozyme patterns of acid phosphatase and alkaline phosphatase in metacercariae and in adults of F. seoulensis by enzyme-histochemistry method and electrophoresis. Acidphosphatase showed a strong activity at pH 5 in the intestinal caecum of adults, but showed no reactions in the nonsubstrate control and in the inhibitor-treated control. Alkaline phosphatase showed a strong activity at pH 8 in the intestinal caecum and the tribocytic organ of adults, and in the intestinal caecum and in the genital anlagen of metacercariae. In non-denature PAGE, ten bands of protein fraction from the extracts of metacercariae and twenty-two bands from adults were detected. In denature PAGE, two protein bands having molecular weights of 192 kDa and 123 kDa were detected in the metacercariae, but absent from adult stage. In adults, protein fractions of 27.5 kDa, 24.5 kDa, 21.4 kDa, 18 kDa, 16 kDa and 15 kDa were detected. In non-denature PAGE, isozymes of acid phosphatase showed the most strong activity at pH 5, whereas no activity was shown at pH 2 and pH 7. One isozyme 85 kDa, 73 kDa and 62 kDa) in adults.

• 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.