• Journal of Life Science
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• v.21 no.1
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• pp.31-35
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• 2011

Dual-specificity protein phosphatases (DUSPs) constitute a family of protein phosphatase characterized by the ability to dephosphorylate phospho-tyrosyl and phospho-seryl/threonyl residues. Most DUSPs are involved in regulation of cell survival and differentiation. In this study, a human dual-specificity protein phosphatase, DUSP28, was isolated from a human kidney cDNA. The recombinant protein was successfully produed in E.coli and showed sufficient phosphatase activity toward DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate). Various phosphatase inhibitors and divalent metals were tested for their effects on the DUSP28 phosphatase activity. As a result, $Zn^{2+}$ was found to strongly inhibit DUSP28 phosphatase activity, suggesting DUSP28 is involved in Zn-related signal transduction pathway. Furthermore, the DUSP28 protein preferred phospho-tyrosyl residues to phospho-threonyl residues, implying its physiological roles in the cellular process.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1996.04a
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• pp.218-218
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• 1996

Brazilin은 포도당 수송을 증가시키는 물질로 autooxidation에 의하여 산화되면서 hydrogen peroxide를 생성할 것으로 추정되었으며, hydrogen peroxide는 phosphatase를 억제하여 포도당 수송을 증가시키는 것으로 보고되었다. 따라서 본 실험에서 brazilin의 산화에 의한 hydrogen peroxide의 생성여부를 확인하고 phosphatase 활성에 미치는 braziline의 작용을 살펴보았다. 먼저 UV absorption spectra를 이용하여 brazilin이 반응액중에서 구조적인 변화를 일으키는지 확인하였다. Hydrogen peroxide의 생성은 rhodamine 123를 이용한 형광측정법으로 측정하였으며, phosphatase의 활성은 pH에 따른 phosphatase의 활성을 p-NPP의 탈인산화의 UV 흡광도 변화로 측정하였다. PP2A의 활성은 phosphorylase a를 기질로 하여 측정하였다.

• Parasites, Hosts and Diseases
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• v.31 no.2
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• pp.165-168
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• 1993

In order to know the enzyme activities of Filbricola seouzenis, an intestinal trematode of human and rodent in Korea. the enzyme histochemical method is applicated. Activities of acid phosphatase (E.C.3.1.3.2) and non-specific esterase (E.C.3.1.1) were present in microvilli and glandular cells of trlbocytic organ and the epithelium of the caecum.

• Journal of Animal Science and Technology
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• v.51 no.2
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• pp.177-182
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• 2009

The glycosylated human MINPP (multiple inositol polyphosphate phosphatase), which was recombinantly over-expressed by using industrial host, Pichia pastoris, showed the phytase activity against phytate ($InsP_6$) and the enzyme activity of the unglycosylated counterpart was decreased to 30%. The optimal phytase activity occurred at pH 7.4. The human MINPP showed high substrate specificity for $InsP_6$ with little activity on other organic phosphate conjugates such as para-nitrophenylphosphate (pNPP), ATP, and ribose-1-phosphate (R-1-P). The phosphatase activity against 2,3-bisphosphoglycerate (2,3-BPG) by human MINPP was increased to 1.2-fold in the presence of stimulator, 1 mM 2-phosphoglycolate (2-PG) but the phytase activity against $InsP_6$ was not affected by addition of 1 mM 2-PG. The phosphatase activity against 2,3-BPG by human MINPP was not increased in the presence of 2 mM $Mg^{2+}$ or 100 mM $Cl^-$.

• Journal of Plant Biology
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• v.35 no.4
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• pp.333-338
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• 1992

Ginkgo (Ginkgo biloba L.) seeds were analyzed to determine the level of soluble sugars and insoluble starch during germination. Also the activities of the hydrolytic enzymes such as amylase, invertase and phosphatase were compared. As amylase activity was sharply increased, significant decline of starch was observed in the female gametophyte and increase of soluble sugars occurred concurrently. Invertase activity was gradually increased in cotyledon and radicle, while it was very low in dry seeds. In addition, phosphatase activity was variable only in radicle, and acid phosphatase showed higher activity than alkaline phosphatase.hatase.

• The korean journal of orthodontics
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• v.27 no.4 s.63
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• pp.599-605
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• 1997

The propose of this study was to evaluate the effect of cellular activity on PDL cells dependent on intermittent and continuous compressive force by determining the alkaline phosphatase activity. An intermittent and continuous compressive forces were applied on PDL cells at the confluent stage. The alkaline phosphatase activity was measured on control and experimental groups every 24, 48, 72hours. The experimental group were consist of continuous and intermittent compressive group which were compressed by $300g/cm^2$ of diaphram pump. The intermittent compressive group was connected by timer which was worked on 10 minutes and off 10minutes. The results were as follows ; 1. The alkaline phosphatase activity of intermittent compressive group was lower than control group at 24 hours(P<0.05). 2. The alkaline phosphatase activity between each groups showed no significant differences at 48hours. 3. The alkaline phosphatase activity of continuous compresssive group was significantly higher than control group at 72 hours(P<0.01).

• The Korean Journal of Zoology
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• v.35 no.1
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• pp.102-106
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• 1992

진도개와 삽사리 혈청 lactate dehydrogenase와 혈청 alkaline phosphatase의 동위효소 및 효소활성도를 분석하였다. 전기영동결과 진도개와 삽사리의 혈청에서는 5두지 종류의 LDH의 동위효소가 모두 확인되었다. LDH의 활성도는 진도개의 경우 522.53 $\pm$ 279.96(U/L)이었고 삽사리는 534.10 $\pm$ 280.35(U/L)이었다. 진도개와 삽사리의 혈청 alkaline phosphatase전기 영동상에서 는 한 종류의 동위효소만 관찰되었고 활성도는 진도개의 경우 7.61 $\pm$ 4.52(K-A unit)였고 삽사리는 10.46 $\pm$ 7. 10(K-A unit) 였다. 삽사리의 ALP 활성도는 연령에 따라 커다란 차이를 나타내었다.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.85-90
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• 1997

The Isozyme activities of Lentinula edodes were studied as a preliminary study for genetic analysis after protoplast fusion. The presence of peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ was examined. An intracellular buffer-soluble protein from the mycelia was used for enzyme analysis on nondenaturing polyacrylamide gels. The auxotrophs of Lentinula edodes were positive for peroxidase, esterase, superoxide dismutase and acid phosphatase. However, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ were not detected. The esterase and peroxidase were not affected by the various culture age. Isozyme identification may be a useful tool after protoplast fusion.

• The Korean Journal of Zoology
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• v.27 no.1
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• pp.1-12
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• 1984

In order to investigate the alkaline phosphtase activities in the mouse oocytes in matuation and preimplantation embryos in developing in culture, the enzyme activities were measured by means of biochemical method. The in vitro effect of levamisole which is known as an inhibitor of the lakaline phosphatase was also observed on the oocyte in maturation and the embryos in early embryogenesis. The results obtained were as follows: The enzyme activity was not detected in the embryos unitl the stage of 4-cell, but it appeared first in the 4-cell embryos and the level of the activity was steady through up to the blastocyst. Levamisole inhibited the alkaline phosphatase activity in the blastocyst, and the activity decreased by almost 70% at 10 mM and 50% at 1 mM as compared with the control. In addition, levamisole inhibited completely the formation of polar body by the oocytes. and induced degeneration of the preimplantation embryos at the dose of 0.5 mM or higher.

• 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.