• 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 Korean Journal of Zoology
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• v.22 no.2
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• pp.67-81
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• 1979

Eelctron microscopic cytochemical methods reveal that acid phosphatase activity appears exclusively in vacuoles surrounding established symbiotes. However, copius amounts of acid phosphatase reaction product are visible between and around some of the degenerating symbiotes in the amebae after treatment of chloramphenicol. It is thought that bacteriostasis by chloramphenicol has served to lost the symbiotic interference to intracellular digestion by the ameba and possibly phodphatase enxymes have been implicated in phagocytosis and intracellular digestion of the symbiotic bacteria.

• 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

• Proceedings of the Botanical Society of Korea Conference
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• 1999.04a
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• pp.9-9
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• 1999

• 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

• 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.

• Korean journal of applied entomology
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• v.15 no.4 s.29
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• pp.169-178
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• 1976

The concentration of amino acids, total nitrogen, trehalose, lipids and the activities of respiratory, acid$\cdot$alkaline phosphatase, glutamic oxalozcetic transaminase and glutamic pyruvic transaminase during larval stage in Pine leaf gall midge, Thecodiplosis janensis Uchi. et Inouye were measured using Paper chromatographic method, micro-Kjeldahl method, Thin layer chromatographic method, Warburg's manometric method, Bessey-Lowry method and Reitman-Frankel method, respectively. Healthy specimens )yore chosen as samples of each larval stages; alrva in gall and larva in soil. Amino acids present in the alcoholic extracts were alanine, glutamic acid, glycine, histidine, methionine, proline, threonine, tryptophan and valine. The total nitrogen concentration reached to 31.348mg/g during the larva in gall and the larval stage in soil of the value was decreased to 29.027mg/g. The hemolymph sugar, trehalose value for larva in soil was about two times of the value for larva in gall. Total lipid, phospholipid,monoacylglycerol, triacylglycerol, sterol, free fatty acid and ester cholesterol were identified at larval stages in gall and soil. Triacylglycerol concentration reached high level in contrast with other lipid contents during larvae in gall and larva in soil. Free fatty acid, sterol except decreased lipids during larval stage in soil. Endogenous respiration, succinate of respiratory activities decreased at larval stage in soil compare with larva in gall. The activities of acid phosphatase decreased larval stage in soil but the activities of alkaline phosphatase increased remarkably. The activities of glutamic oxaloacetic transaminase and glutamic pyruvic transaminase reached high level of the larva in gall.

• Korean Journal of Food Science and Technology
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• v.28 no.4
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• pp.663-667
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• 1996

Acid phosphatase (EC 3.1.3.2) from Welsh onion was partially purified by Sephacryl S-200 gel filtration and CM-Sepharose CL-6B ion exchange chromatography. The optimum pH and temperature of acid phosphatase from green onion were pH 5.5 and $60^{\circ}C$, respectively. The enzyme was the most stable at pH 6.0 and unstable above pH 9.0. The activation energy of the enzyme was determined to be 4.86kcal/mole. The enzyme utilized p-nitrophenyl phosphate most as a best substrate among tested possible substrates, while 5'-GMP and 5'-IMP were poor substrates for the enzyme. $K_{m.app.}$ of the enzyme with p-nitrophenyl phosphate as a substrate was identified as 0.87mM. Among metal ions and inhibitors tested, $Cr^{+++},\;Zn^{++},\;Cu^{++}$, molybdate and metavanadate ions inhibited the enzyme reaction drastically.

• Korean Journal of Soil Science and Fertilizer
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• v.30 no.2
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• pp.189-195
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• 1997

A phosphate solubilizing bacterium (PSB) possessing a high ability to solubilize hydroxyapatite (HA) was isolated from the rhizosphere of wheat. The PSB markedly developed clear zones after inoculating for 36 hours at $30^{\circ}C$. This bacterium was identified as Enterobacter agglomerans through API 20E system and Biolog$^{TM}$ analysis. The values of similarity and distance coefficient from authentication trial of the strain were 0.656 and 4.79 respectively. High performance liquid chromatography (HPLC) of the products of this strain indicated that this strain excretes maily oxalic acid with som other organic acids. During the incubation period of E. agglomerans, the pH values showed an inverse correlation ($r^2=0.933^{**}$) with solubilization of inorganic phosphate. Acid phosphatase activity of the strain was 10-15 times greater than alkaline phosphatase activity. Alkaline phosphatase activity had almost constant near zero activity across time. The population of E. agglomerans greatly increased during the first day of inoculation ; however, it drastically decreased thereafter.

• 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