• 제목/요약/키워드: pH dependent

검색결과 1,768건 처리시간 0.03초

Resistance of Cementitious Binders against a Fall in the pH at Corrosion Initiation

  • Song, Ha-Won;Jung, Min-Sun;Ann, Ki Yong;Lee, Chang-Hong
    • Corrosion Science and Technology
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    • 제8권3호
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    • pp.110-115
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    • 2009
  • At the onset of corrosion of steel in concrete, hydrogen ions usually evolve in the process of electrochemical reaction, thereby decreasing the pH of the pore solution, which can be buffered by cement hydration products, as being representatively illustrated by calcium hydroxide. Hence, a fall in the pH is dependent on properties of cement hydration (i.e. hydration products and degree of hydration). The present study tested acid neutralization capacity (ANC) of cementitious binders of OPC(Ordinary Portland Cement), 30% PFA(Pulverized Fuel Ash), 60% GGBS(Ground Granulated Blast Furnace Slag), 10% SF(Silica Fume) to quantify the resistance of cement matrix to a pH fall. Cement pastes were cast at 0.4 of a free W/C ratio with 1.5% chlorides by weight of binder in cast. Powder samples obtained crushed and ground specimen after 200 days of curing were diluted in still water combined with different levels of 1M nitric acid solution, ranging from 0.5 to 20 mol/kg. Then, the pH of diluted solution was monitored until any further change in the pH did not take place. It was seen that the pH of the diluted solution gradually decreased as the molar amount of nitric acid increased. At some particular values of the pH, however, a decrease in the pH was marginal, which can be expressed in the peak resistances to a pH fall in the ANC curve. The peaks occurred at the variations in the pH, depending on binder type, but commonly at about 12.5 in the pH, indicate a resistance of precipitated calcium hydroxide. The measurement of water soluble chloride at the end of test showed that the amount of free chloride was significantly increased at the pH corresponding to the peaks in the ANC curve, which may reflect the adsorption of hydration products to chlorides.

녹차 카테킨류의 pH에 대한 안정성 연구 (Effect of pH on the Stability of Green tea Catechins)

  • 박영현;원은경;손동주
    • 한국식품위생안전성학회지
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    • 제17권3호
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    • pp.117-123
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    • 2002
  • 시중에 유통되고 있는 녹차중의 catechin류에 대하여 열수추출 및 HPLC분석을 통하여 함량을 조사하고 이를 효율적으로 이용하기 위하여 pH조건이 녹차 catechin류의 안정성에 미치는 영향에 대하여 분석하였다. 시판 중인 전남 보성산 녹차의 catechin류 함량은 (+)-catechin>(-)-EGCg>(-)-EGC>(-)-EC>(-)-ECg순으로 추출되었고 Total catechin류의 함량은 103.72mg/g이었다. 녹차에서 분리·정제되어진 catechin류인 (+)-catechin, (-)-EC, (-)-ECg, (-)-EGCg를 pH 3∼11에 대한 안정성을 흡광도측정장치를 이용하여 측정하였다. 그 결과 catechin류의 pH에 대한 영향을 최대흡수파장 및 흡광도 변화로 보면 pH가 높을수록 (+)-catechin과 (-)-EC은 흡광도가 증가되었고 (-)-ECg와 (-)-EGCg는 최대흡수파장이 증가되었다. 또한 7일간 실온에서 저장하면서 기간에 따른 변화를 살펴본 결과에서 산성조건에서는 큰 변화가 없지만 알칼리조건에서는 흡광도가 증가되었다. (+)-catechin과 (-)-EC은 알칼리조건에서 흡수파장 400∼430 nm에서 저장기간이 길수록 흡광도가 증가되었다. 이는 녹차의 갈변과 관계가 있을 것으로 생각되었다. 이상의 결과로, 녹차 Catechin유도체의 pH 및 저장기간에 대한 영향은 ECg, EGCg에 gallic acid의 결합에 의한 것으로 생각되고, C, EC의 불안정은 중합반응으로 생각된다. 녹차 catechin류는 대부분 산성에서 저장기간이 길고 안정한 것으로 나타났으나 생리활성이 강한 (-)-EGCg는 산성에서도 불안정한 것으로 나타났다. 결론적으로 녹차의 기능성 성분을 효율적으로 이용하기 위해서는 pH를 낮게 유지하여야 할 것으로 사료되어진다.

FeS 수용액 내 pH에 따른 5가비소의 반응 메커니즘 연구 (Mechanistic Study of FeS Reacted with Arsenate under Various pH Conditions)

  • 한영수;이무열;성혜진
    • 한국지하수토양환경학회지:지하수토양환경
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    • 제27권1호
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    • pp.25-30
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    • 2022
  • Mackinawite (FeS), as a ubiquitous reduced iron mineral, is known as a key controller of redox reactions in anaerobic subsurface environment. The reaction of FeS with redox-sensitive toxic element such as arsenic is substantially affected by pH conditions of the given environments. In this study, the interaction of As(V) with FeS was studied under strict anaerobic conditions with various pH conditions. The pH-dependent arsenic removal tests were conducted under wide ranges of pH conditions and X-ray absorption spectroscopy (XAS) was applied to investigate the reaction mechanisms under pH 5, 7, and 9. The removal efficiency of FeS for As(V) showed the higher removal of As(V) under low pH conditions and its removal efficiency decreased with increasing pH, and no As(V) reduction was observed in 1 g/L FeS solution. However, XAS analysis indicated the reduction of As(V) to As(III) occurred during reaction between FeS and As(V). The reduced form of As(III) was particularly identified as an arsenic sulfide mineral (As2S3) in all pH conditions (pH 5, 7, and 9). As2S3 precipitation was more pronounced in pH 5 where the solubility of FeS is higher than in other pH conditions. The linear combination fitting results of XAS demonstrated that As(V) removal mechanism is concerted processes of As2S3 precipitation and surface complexation of both arsenic species.

Sodium fluoride와 Sodium orthovanadate가 조골세포주 MC3T3-E1에 미치는 영향에 관한 연구 (THE EFFECT OF SODIUM FLUORIDE AND SODIUM ORTHOVANADATE ON OSTEOBLASTIC CELL LINE MC3T3-E1 CELLS)

  • 김원진;정규림
    • 대한치과교정학회지
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    • 제21권1호
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    • pp.97-111
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    • 1991
  • It is the aim of this study to investigate the effects of sodium fluoride and sodium orthovanadate upon the proliferation and activity of the osteoblast (MC3T3-E1 cells). MC3T3-E1 cells were cultured in $\alpha-MEM$ containing $10\%$ FBS and various concentration of sodium fluoride and sodium orthovanadate was appended to serum free media. DNA synthesis was examined through the $[^3H]$ thymidine incorporation into DNA. Collagen synthesis was examined through the $[^3H]$ proline incorporation into collagenase digestible protein and noncollagen protein. The following results were drawn; 1. Sodium fluoride stimulated the DNA synthesis of osteoblast significantly in dose-dependent manner within the concentration from $2{\mu}M$ to $10{\mu}M$ (P < 0.005). 2. Sodium orthovanadate stimulated the DNA synthesis of osteoblast significantly in dose-dependent manner within the concentration from $2{\mu}M\;to\;8{\mu}M$, however showed diminution at $10{\mu}M$ (P < 0.001). 3. Sodium fluoride and sodium orthovanadate stimulated the percent collagen synthesis of osteoblast significantly in dose-dependent manner within the concentration from $5{\mu}M$ to $10{\mu}M$ (P < 0.001). 4. Sodium fluoride and sodium orthovanadate stimulated the noncollagen synthesis of osteoblast significantly in dose-dependent manner within the concentration from $5{\mu}M\;to\;10{\mu}M$ (P < 0.001). In conclusion, sodium fluoride and sodium orthovanadate stimulate the proliferation and activity of osteoblast by stimulation of DNA synthesis and collagen and noncollagen synthesis in osteoblast.

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Effects of Amifostine on Apoptosis, Cell Cycle and Cytoprotection of Human Colon Cancer Cell Lines

  • Eun Ju Lee
    • 대한의생명과학회지
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    • 제29권4호
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    • pp.287-295
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    • 2023
  • Amifostine was developed to protect cells, but it is known to induce cytotoxicity and apoptosis, and the exact mechanism is unknown. In this study, we investigated how the DNA mismatch repair (MMR) system interacts with p53 to prevent apoptosis, cell cycle arrest, and cytoprotective effects induced by amifostine. HCT116 colon cancer cells sublines HCT116/p53+,HCT116/p53+, HCT116/p53-, HCT116/E6 and HCT116+ch3/E6 cells were used for evaluation. Amifostine induced G1 arrest and increased toxicity two-fold in p53- cells regardless of MMR expression. Both G1 cell cycle arrest and induction of p53 protein peaked at 24 h after the start of amifostine exposure. Both G1 cell cycle arrest and induction of p53 protein peaked at 24 h after the start of amifostine exposure. Amifostine induced the expression of p21 protein in both p53+ and p53- cells. As for apoptosis, compared to p53- cells, p53+ cells showed 3.5~4.2 times resistance to amifostine-induced apoptosis. HCT116+E6 with both p53 and MMR loss showed maximum apoptosis at 48 h, and HCT116+ch3/E6HCT116+ch3/E6 with p53 loss showed maximum apoptosis at 24 h. As a result, it was confirmed through in vitro experiments that amifostine-induced G1 cell cycle arrest and apoptosis are mediated through a pathway dependent on MMR and p53 protein.

황산철 도금액 중 Si 입자의 공석 특성 (Co-deposition of Si Particles During Electrodeposition of Fe in Sulfate Solution)

  • 문성모;이상열;이규환;장도연
    • 한국표면공학회지
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    • 제37권6호
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    • pp.319-325
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    • 2004
  • Fe thin films containing Si particles were prepared on metallic substrates by electrodeposition method in sulfate solutions and the content of codeposited Si particles in the films was investigated as a function of applied current density, the content of Si particels in the solution, solution pH, solution temperature and concentration of $FeSO_4$$7H_2$O in the solution. The amount of Si codeposited in the film was not dependent on the applied current density, solution pH and solution temperature, while it was dependent on the content of Si particles in the solution and the concentration of $FeSO_4$$7H_2$O in the solution. The amount of Si codeposited in the film increased with increasing content of Si particles in the solution but reached a maximum value of about 6 wt% when the content of Si particles in the solution exceeds 100 g/l. On the other hand, the content of Si codeposited in the film increased up to about 17 wt% with decreasing concentration of $FeSO_4$$7H_2$O in the solution. These results would be applied to the fabrication of very thin Fe-6.5 wt% Si sheets for electrical applications.

Multiple Actions of Dimethylsphingosine in 1321N1 Astrocytes

  • Lee, Yun-Kyung;Kim, Hyo-Lim;Kim, Yu-Lee;Im, Dong-Soon
    • Molecules and Cells
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    • 제23권1호
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    • pp.11-16
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    • 2007
  • N,N-dimethyl-D-erythro-sphingosine (DMS) is an N-methyl derivative of sphingosine and an inhibitor of protein kinase C (PKC) and sphingosine kinase (SK). In the present study, we examined the effects of DMS on intracellular $Ca^{2+}$ concentration, pH, and glutamate uptake in human 1321N1 astrocytes. DMS increased intracellular $Ca^{2+}$ concentration and cytosolic pH in a concentration-dependent manner. Pretreatment of the cells with the $G_{i/o}$ protein inhibitor PTX and the PLC inhibitor U73122 had no obvious effect. However, removal of extracellular $Ca^{2+}$ with the $Ca^{2+}$ chelator EGTA or depletion of intracellular $Ca^{2+}$ stores with thapsigargin impeded the DMS-induced increase of intracellular $Ca^{2+}$ concentration. Pretreatment of cells with $NH_4Cl$ or monensin reduced the DMS-induced $Ca^{2+}$ increase. However, inhibition of the DMS-induced $Ca^{2+}$ increase with BAPTA did not influence the DMS-induced pH increase. DMS also inhibited glutamate uptake by the 1321N1 astrocytes in a concentration-dependent manner. It also increased intracellular $Ca^{2+}$ and pH in PC12 neuronal cells. Our observations on the effects of DMS on 1321N1 astrocytes and PC12 neuronal cells point to a physiological role of DMS in the brain.

Dephosphorylation of p53 Ser 392 Enhances Trimethylation of Histone H3 Lys 9 via SUV39h1 Stabilization in CK2 Downregulation-Mediated Senescence

  • Park, Jeong-Woo;Bae, Young-Seuk
    • Molecules and Cells
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    • 제42권11호
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    • pp.773-782
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    • 2019
  • Cellular senescence is an irreversible form of cell cycle arrest. Senescent cells have a unique gene expression profile that is frequently accompanied by senescence-associated heterochromatic foci (SAHFs). Protein kinase CK2 (CK2) downregulation can induce trimethylation of histone H3 Lys 9 (H3K9me3) and SAHFs formation by activating SUV39h1. Here, we present evidence that the PI3K-AKT-mTOR-reactive oxygen species-p53 pathway is necessary for CK2 downregulation-mediated H3K9me3 and SAHFs formation. CK2 downregulation promotes SUV39h1 stability by inhibiting its proteasomal degradation in a p53-dependent manner. Moreover, the dephosphorylation status of Ser 392 on p53, a possible CK2 target site, enhances the nuclear import and subsequent stabilization of SUV39h1 by inhibiting the interactions between p53, MDM2, and SUV39h1. Furthermore, $p21^{Cip1/WAF1}$ is required for CK2 downregulation-mediated H3K9me3, and dephosphorylation of Ser 392 on p53 is important for efficient transcription of $p21^{Cip1/WAF}$. Taken together, these results suggest that CK2 downregulation induces dephosphorylation of Ser 392 on p53, which subsequently increases the stability of SUV39h1 and the expression of $p21^{Cip1/WAF1}$, leading to H3K9me3 and SAHFs formation.

Evidence for two $Na^+$/$H^+$ Antiport Systems in Escherichia coli

  • Seo, Sung-Yum
    • 미생물학회지
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    • 제30권4호
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    • pp.269-277
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    • 1992
  • Several insertion mutants of Escherichia coli in the ant gene, coding for $Na^{+}$ $H^{+}$ antiport activity, showed littel, if any, reduction in the antiport activity. $Na^{+}$ dependent transport activity also remained at wild type level. These facts led to the idea that E. coli has evolved at least two distinct systems for extrusion of $Na^{+}$ The antiport activities were studied under various conditions to reveal different properties of these systems. For convenience these activities are referred to as major and minor activities. The distinguishing properties of the two systems include : kinetics (Km, Vm) at pH 7.8, competition pattern between $Na^{+}$ and Li$^{+}$ , pH profiles, pattern of the change in kinetic parameters as a function of pH, and sensitivity to protease, chemicals and heat.

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Gonadotropins, Prostaglandin $F_{2{\alpha}}$ 및 Ouabain이 황체막의 $Ca^{++}-ATPase$ 활성도에 미치는 영향 (Effects of Gonadotropins, Prostaglandin $F_{2{\alpha}}$, and Ouabain on the $Ca^{++}-ATPase$ Activity in Luteal Membranes)

  • 구본숙;김인교
    • The Korean Journal of Physiology
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    • 제21권1호
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    • pp.47-58
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    • 1987
  • It has been reported that the luteal function may be regulated by the intracellular $Ca^{++}$ level which may be adjusted partially by the high affinity $Ca^{++}-ATPase$ in luteal cell membranes. Then, one may expect that luteotropic and/or luteolytic agents, such as gonadotropins, prostaglandin $F_{2{\alpha}}\;(PGF_{2{\alpha}})$ and ouabain, affect the intracellular $Ca^{++}$ level. In this present study, therefore, we examined the effects of luteinizing hormone (LH, or human chorionic gonadotropin, hCG), $PGF_{2{\alpha}}$ and ouabain on the kinetic properties of the high affinity $Ca^{++}-ATPase$ in light membrane, heavy membrane, and microsomal fractions from the highly luteinized ovary. LH (or hCG) increased the affinity and the Vmax for $Ca^{++}$ both in light membrane and heavy membrane. $PGF_{2{\alpha}}$ increased the Vmax in light membrane and decreased the Km in heavy membrane for $Ca^{++}$ at low concentration $(5\;{\mu}g/ml)$. At higher concentration, however, $PGF_{2{\alpha}}$ oppositly affected on kinetic properties, that shown at low concentration. Ouabain, a potent inhibitor of $Na^+-K^+-ATPase$, increased the Km at high concentration $(10^{-4}\;M)$, however, decreased the Vmax for $Ca^{++}$ in light membrane at low concentration $(10^{-6}\;M)$. Also, ouabain increased the Km for $Ca^{++}$ in heavy membrane without changes in the Vmax at both concentrations. It seems that LH and low dose of $PGF_{2{\alpha}}$ increase the intracellular $Ca^{++}$ level and cause in activation of $Ca^{++}-ATPase$, however, higher dose of $PGF_{2{\alpha}}$ and ouabain inhibit directly $Ca^{++}-ATPase$ activity and result in increase in intracellular $Ca^{++}$ level. According to the above results, we suggest that luteotropic and/or luteolytic agents regulate the luteal progesterone $(P_4)$ production through two different pathways; one is cyclic adenosine monophosphate (cAMP)-dependent and another is $Ca^{++}-dependent$. Intracellula. $Ca^{++}$ level regulated by the high affinity $Ca^{++}-ATPase$ may affect both pathways in a time-dependent fashion. LH (or hCG) acts on the luteal $P_4$ production via both pathways. The initial step is $Ca^{++}$ dependent, and the late step is cAMP dependent. $PGF_{2{\alpha}}$ and ouabain increase the intracellular $Ca^{++}$ concentration so that basal luteal $P_4$ production is increased and LH-stimulated $P_4$ production is inhibited by the inhibiting LH-dependent adenylate cyclase activity.

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