• 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.

• Proceedings of the Korean Environmental Sciences Society Conference
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• 2006.11a
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• pp.301-303
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• 2006

조사해역에서의 Phosphatase에 의한 최대분해속도(Vmax)는 $0.26\;{\sim}\;7.09{\mu}M/L/hr$ 로서, 식물플랑크톤 bloom을 보였던 6월27일 조사 시에 높게 나타났으며 수온이 하강하고 클로로필 농도가 낮았던 9월13일 조사결과에서 가장 낮게 나타났다. 식물플랑크톤에 의한 유기 인산염 분해를 알아보기 위해 Specific activity를 구하였다. Phosphatase activity와 Chlorophyll. a의 변화는 유사한 변화를 보여주고 있으며, 이는 식물플랑크톤 이 Phosphatase의 분비에 큰 기여를 하는 것으로 나타났다.

• 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.

• Journal of Veterinary Clinics
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• v.7 no.1
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• pp.429-438
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• 1990

The cytochemical characteristics of the hematopoietic cells in blood and bone marrow from 3 clinically healthy dogs were examined using a battery of cytochemical stains. Alkaline phosphotase activity was demonstrated in eosinophilic series and occassionally in progranulocytes. A variety of cells exhibited acid phosphatase activity, but tartrate-resistant acid phosphatase activity was seen only in eosinophilic series. Peroxidase activity was observed in myeloblasts to segmented cells of granulocytic series and in monocytes. ${\alpha}$-naphthyl acetate esterase activity was found in monocytes and occassionally in lymphocytes. Naphthyl-AS-D-chloroacetate esterase marked neutrophilic series from myeloblasts to segmented cells. ${\beta}$-Glucuronidase activity was detected in a variety of cells except the cells of erythrocytic series. Periodic acid Schiff stain-positive granules were demonstrated in the neutrophilic and eosinophilic series from myelocytes to segmented cells and in monocytes and occassionally in lymphocytes. Sudan black B stain-positive granules marked granulocytic series from myeloblasts to segmented tells and monocytes.

• Environmental Analysis Health and Toxicology
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• v.17 no.1
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• pp.73-80
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• 2002

Pyruvate dehydrogenase phosphatase (PDP)와 kinase는 당대사시 해당과정에서의 대사 산물인 pyruvate를 acetyl CoA로 만들어 구연산 회로로 진입시켜 주는 효소인 pyruvate dehydrogenase complex (PDC)의 활성을 조절하는 중요한 효소이다. PDP의 catalytic subunit는 PDC의 dihydrolipoamide acetyltransferase (E2), PDP regulatory subunit (PDPr), 그리고 칼슘 결합 도메인 등으로 구성되어 있는 것으로 추측되어지고 있다. 본 연구에서는 그 구조와 기능과의 상관관계를 알아보기 위해 PDPc를 E. coli JM101에서 발현시켜 순수 정제 후 단백분해 효소를 이용한 제한적 가수분해 방법을 이용해 그 구조와 기능과의 상관관계에 대해 연구하고자 하였다 정제된 PDPc는 trypsin, chymotrypsin, Arg-C 그리고 elastase를 이용하여 3$0^{\circ}C$ 그리고 pH 7.0에서 제한적으로 분해시켰으며 각 분해산물의 아미노 말단의 아미노산 배열을 분석하였다. 그 결과 PDPc는 trypsin, chymotrypsin, elastase에 의해 N-terminal의 50 kD과 C-terminal의 10 kD의 두개의 분해산물을 만들었으며, Arg-C에 의해 50kD의 분해산물은 약 35kD와 15kD으로 더 가수분해가 되었다. 이러한 결과로 볼 때 PDPc는 앞에서 추측한데로 세개의 주요한 기능적 도메인으로 이루어져 있음을 알 수 있었다 또한 C-terminal의 10kD은 PDPc의 활성에는 영향을 주지 않는 것으로 밝혀졌으나 다른 도메인의 기능은 더 연구가 되어져야 할 것으로 생각된다.

• 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.

• 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).

• Journal of Veterinary Clinics
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• v.14 no.1
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• pp.65-69
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• 1997

The bone alkaline phosphatase(BALP) in 130 sera of normal dogs were assayed according to the lectin precipitation method of Rosalki and Foo. The serum BALP activities showed a wide variation as $23.27({\pm}14.73)$ IU/L in young dogs from 6weeks to 12 months old and were lower in magnitude as $9.24({\pm}3.36)$ IU/L in elder dogs from 1 years to 6years old. The serum BALP activities in normal dogs were no significant correlation in sex.

• The Journal of the Korean bone and joint tumor society
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• v.7 no.2
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• pp.41-50
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• 2001

Purpose : To investigate biochemical markers for osteosarcoma, activities of deoxyribocuclease(DNase), ribonuclease(RNase), 5'-nucleotidase, alkaline phosphatase and amylase were determined in the osteosarcoma tissue and serum of patients with osteosarcoma. Also studied were DNase, RNase in osteosarcoma tissue, isolating the enzymes from the sarcoma tissue and investigating the sarcoma specific enzymes. Materials and Methods : The experimental tissue and serum were obtained from twelve patients with osteosarcoma. The control group were obtained from the normal healthy tissue of the same patients. The tissue were centrifugalized to obtain extracts. The extracts were analized for the estimation of nucleic acid, protein contents and enzyme activities. And then each enzymes were isolated and analized by DEAE-cellulose chromatography and estimated for activities. Result : Activities of acid DNase, RNase, 5'-nucleotidase and alkaline phosphatase were significantly increased in osteosarcoma tissue. Neutral RNase in osteosarcoma tissue was shown to bo highly active, exhibiting secretory form of RNase inhibitor associated with the RNase was also increased. In the serum of patients with osteosarcoma, RNase activity was significantly increased. DEAE-cellulose column chromatographical analysis revealed that acid DNase was isolated as a single enzyme and neutral RNase as five isozymes in osteosarcoma tissue. Conclusion : The results indicated that combination of these enzymes could be used as markers for osteosarcoma. The results indicated that acid DNase and neutral RNase might play a role in genesis of sarcoma and suppression of sarcoma.

• 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.