• Fisheries and Aquatic Sciences
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• v.13 no.1
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• pp.49-55
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• 2010

A bacterial strain with phytase and glucose-1-phosphatase activity was isolated from seawater. The colony was identified as an Enterobacter cloacae strain and named E. cloacae B11. A gene, agpEnB11, coding for an intracellular acid glucose phosphatase was cloned from the strain and sequenced. It comprised 1,242 nucleotides and encoded a polypeptide of 413 amino acids. Recombinant glucose-1-phosphatase (AgpEn) was overexpressed in Escherichia coli and purified using Ni-NTA column under native conditions. Purified protein displayed a single band of 47 kDa on SDS-PAGE. AgpEn hydrolyzed a wide variety of phosphorylated compounds, with high activity for glucose-1-phosphate and glucose-6-phosphate. Optimum pH and temperature for enzyme activity were pH 5.0 and $50^{\circ}C$, respectively. Enzyme activity was stimulated by $Ca^{2+}$ and $Co^{2+}$, and inhibited by $Cu^{2+}$.

• Korean Journal of Veterinary Service
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• v.34 no.4
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• pp.397-401
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• 2011

Aspiration of lytic bone lesions is an excellent diagnostic test in the initial evaluation of primary bone tumor. However, cytologically, it can be difficult to differentiate osteosarcoma (OSA) from other bone neoplasms, including fibrosarcoma, chondrosarcoma, synovial cell sarcoma, malignant fibrous histiocytoma and malignant peripheral nerve sheath tumor. The purpose of this study is to introduce alkaline phosphatase (ALP) staining to differentiate OSA from other mesenchymal tumors. Tumors actively producing bone are specifically positive for ALP staining. Unstained, cytologic specimens were incubated for 10 minutes with nitroblue tetrazolium chloride/5-bromo-4-chloro-3-indolyl phosphate toluidine salt-phosphatase substrate. Among 20 cases of cytology specimen, 14 were positive for ALP staining and histopathology, 6 were negative for ALP staining and histopathology. ALP staining was 100% sensitive and specificity for the diagnosis of OSA. Aspirate cytology with ALP staining was a simple, fast, safe and accurate diagnostic test for the evaluation of suspected OSA lesions in dogs.

• The Korean Journal of Zoology
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• v.18 no.4
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• pp.173-180
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• 1975

Activities of serum alkaline phosphatase(SALP) and serum acid phosphatase (SACP) have been assayed in adult male Sprague-Dawley rats acclimated to $30^\\circ C$ and $33^\\circ C$for 240 hours and 64 hours, respectively. The alteration in the activities of SALP and SACP in rats acclimated to $33^\\circ C$ was generally greater than those acclimated to $30^\\circ C$. The SACP and SALP activities of the rats acclimated to $30^\\circ C$ showed generally a persistently high levels in comparison to the control. It may be inferred that the SALP and SACP positibly be involved directly or indirectly in thermoregulation during acclimation to $30^\\circ C$.

• Korean Journal of Breeding Science
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• v.42 no.5
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• pp.455-462
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• 2010

Purple acid phosphatase is important for phosphorus remobilization in plants, but its role in plant adaptation to low phosphorus availability is not known. The cDNA encoding O. sativa purple acid phosphatase (OsPAP1) has 1008 bp with an open reading frame of 335 amino acid residues. The amino acid sequence of OsPAP1 cDNA shows of 50-51% identity with other plant purple acid phosphatases. OsPAP1 was expressed in rice plants and in cell cultures in the absence of phosphate ($P_i$). The expression was organ-specific with the strongest expression in $P_i$-deprived roots. Functional expression of the OsPAP1 gene in the transgenic Arabidopsis line was confirmed by northern and western blot analysis. OsPAP1 overexpression lines had higher phosphatase activity than wild-type. Overexpression of OsPAP1 in Arabidopsis plants resulted in increased Pi accumulation under Pi sufficient condition. These results show that the OsPAP1 gene represents more efficient $P_i$ uptake and can be used to develop new transgenic dicotyledonous plants.

• Molecules and Cells
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• v.42 no.7
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• pp.546-556
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• 2019

Protein phosphatase 4 (PP4) is a crucial protein complex that plays an important role in DNA damage response (DDR), including DNA repair, cell cycle arrest and apoptosis. Despite the significance of PP4, the mechanism by which PP4 is regulated remains to be elucidated. Here, we identified a novel PP4 inhibitor, protein phosphatase 4 inhibitory protein (PP4IP) and elucidated its cellular functions. PP4IP-knockout cells were generated using the CRISPR/Cas9 system, and the phosphorylation status of PP4 substrates (H2AX, KAP1, and RPA2) was analyzed. Then we investigated that how PP4IP affects the cellular functions of PP4 by immunoprecipitation, immunofluorescence, and DNA double-strand break (DSB) repair assays. PP4IP interacts with PP4 complex, which is affected by DNA damage and cell cycle progression and decreases the dephosphorylational activity of PP4. Both overexpression and depletion of PP4IP impairs DSB repairs and sensitizes cells to genotoxic stress, suggesting timely inhibition of PP4 to be indispensable for cells in responding to DNA damage. Our results identify a novel inhibitor of PP4 that inhibits PP4-mediated cellular functions and establish the physiological importance of this regulation. In addition, PP4IP might be developed as potential therapeutic reagents for targeting tumors particularly with high level of PP4C expression.

• The Korean Journal of Zoology
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• v.15 no.4
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• pp.183-191
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• 1972

A histochemical study of the respiratory tract in developing chick was done to demonstrate PAS-postivie materials, ribonucleic acid, phospholipid, and alkaline phosphatase activity. Following results are obtained: 1. The alkaline phosphatase activity was found to be high before the appearance of cartilage in mesenchyme surrounding the tracheal epithelium. The enzyme activity declined after the cartilage formation, followed by the restricted activity in epithelium in the postembryonic stage. 2. A moderate positive reaction of ribonucleic acid was found in the cytoplasm of the epithelium and undifferentiated mesenchyme. As the cartilage grew differentiated the reaction of ribonucleic acid was found to disappear in the mesenchyme surrounding the epithelim, but the cytoplasm of the glands showed a moderate positive reaction. 3. Goblet cells of the mucosa and glandular cells showed highly positive reaction, but the basement membrane exhibited slightly positive PAS-reaction. 4. Epithelial cells of the mucosa showed a weak to moderate reaction. However, the epithelia of bronchiol and alveoli in the differentiating period and glandular cells showed a strong positive reaction in Baker's hematein test.

• The Korean Journal of Physiology
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• v.7 no.1
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• pp.1-11
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• 1973

To study the effects of Korean ginseng on mice visceral alkaline phosphatase activity and inorganic phosphate phosphorus level in the blood, the experimental groups of male and female mice were injected subcutaneously with 0.01 ml or 0.02 ml of Tyrode solution per 10 g of body weight daily, and 0. 1 mg or 0.2 mg of alcohol extract of ginseng which was diluted with Tyrode solution. After groups of mice were treated for 7 days or 14 days, the alkaline phosphatase activity in the jejunum, kidney and liver homogenate and serum were determined with sodium ${\beta}-glycerophophosphate$ as substrate, and quantified the content of inorganic phosphate phosphorus in the blood of above mice. 1. Alkaline phosphatase activity in the jejunum, kidney, liver and serum of male mice for the 7 day treatment with ginseng extract (0.1 mg/10 g) was increased by 15.28%, 12.86%, lg.05% and 11.70% respectively, compared with Tyrode solution group. 2. Alkaline phosphatase activity in the jejunum, kidney, liver and serum of female mice for the 7 day treatment with ginseng extract (0.2 mg/10 g) was increased 3.46%, 6.94%, 20.37% and 4.05 % respectively. 3. Alkaline phosphatase activity in the jejunum, kidney, liver and serum of male mice for the 14 day treatment with ginseng extract(0.1 mg/10 g) was increased·15.92%, 19.76f, 10.16% and -1.63 % respectively. 4. Alkaline phosphatase activity in the jejunum, kidney, liver and serum of female mice for the 14 day treatment with ginseng extract(0.2 mg/10 g) was increased 18.89%, 24.55%, 16.97% and 27.59% respectively. 5. Increasing activity of the enzyme in the liver of both male and female mice for the 7 day treatment was declined to some extent at the 14 day treatment, on the other hand, increasing activity of the enzyme in the jejunum, kidney and serum of mice for the 7 day treatment was more promoted at the 14 day treatment. 6. The 7 day and 14 day treatment with ginseng extract increased 20.20% and 20.96% of inorganic phosphate phosphorus in male blood, 22.38% and 17.57f in female blood respectively. In accordance with the results mutual relationships of ginseng, internal secretion, nucleic acid and alkaline phosphatase activity were disscussed.

• Proceedings of the Korean Biophysical Society Conference
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• 2001.06a
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• pp.20-20
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• 2001

The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals a phosphatase domain similar to protein phosphatases but having an enlarged active site important for the accommodation of the phosphoinositide substrate.(omitted)

• The Korean Journal of Zoology
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• v.31 no.4
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• pp.300-308
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• 1988

Human placental alkaline phosphatase (PLAP), one of the oncofetal antigen was purified from placentas through the procedures including butanol extraction, concanavalin A-Sephar-ose, DEAE-cellulose and Sephadex G-200 gel chromatography. Monoclonal antibodies (fibs) against human PMP were produced by hybridizing SP 210-Ag 14 mouse myeloma cells with spleen ceils of Balblc mice immunized with PLAP. Six stable monoclones uvere obtained by cloning tuvice in serial dilutions, and the monoclonal speclfidty of these MAbs was confirmed by biochemical and immunonogical criteria. Tumor marker의 하나인 태반형 alkaline phosphatase(PLAP)에 대한 단일 클론항체의 생산과 분석을 위하여, 태반조직을 재료로 butanol 추출법 및 concanavaline A-Sepharose, DEAE-cellulose, Sephadex G-200 gel 크로마토그라피법에 의하여 PLAP를 순수 분리하였다. 이를 항원으로 하여 하이브리도마 방법에 의해 항-PLAP 단일 클론항체를 생산 분비하는 안정된 6클론세포를 얻었으며 생화학적 및 면역학적 분석방법으로 이들의 단일 클론성을 확인하였다.

• Microbiology and Biotechnology Letters
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• v.23 no.2
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• pp.131-137
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• 1995

The alkaline phosphatase (K-ALPase) gene of Kluyveromyces fragilis has been cloned (1) and determined its base sequences (2) previously in our laboratory. When the K-ALPase gene was expressed in Escherichia coli and Saccharomyces cerevisiae, it showed a constitutive activity in E. coli, and a derepressed activity in S. cerevisiae in phosphate-limited medium. Northem hybridization experiment was performed to elucidate the transcription level of the K-ALPase gene. Northern experiment showed that transcription level of K-ALPase gene in S. cerevisiae was higher in phosphate depletion, but it was higher in high phosphate medium than in phosphate limited medium in K. fragilis. The transcription initiation site of the K-ALPase gene was determined by primer extension analysis. It matched nucleotide position - 169 in relation to the putative trnslational start site.