• The Korean Journal of Zoology
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• v.34 no.4
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• pp.452-459
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• 1991

담수산 대형 아메바인 각moeba proteus의 위상차 현미경 관찰 및 사진 분석을 통하여 수축포의 배출활동을 조사하f:다. Chalkley's 무기 염류 배양액에 첨가한 0. 1 mM ATP(disodium salt)에 의해 수축포의 배출속도는 270%로 증가하f:으며, 이 ATP의 효과는 Na+ 이온농도가 0.46mM 이상일 때 유효하였다. 실험용액의 NaGl 농도를 10 mM까지 증가시켰을 때 배출작용은 230%에 이르기까지 완만한 직선적 증가를 보였으며, 0.1 mM ATP를 첨가했을 때는 소폭의 NaCl농도 증가(0.50 mM)에 대하여 급격한 상승을 보였다. 이 배출 촉진은 Na+이온에 대해서 선별적으로 이루어졌으며 K+이온으로는 대체될 수 없었다. 배출속도는 Cac12를 제외한 Chalkley's 액에 50 $\mu$ M EDTA(disodium)를 첨가하였을 때에는 2900ye로 증가하였으며 , Caclf 농도가 증가됨에 따라 현격한 감소를 보였다. Chalkley's용액의 Cac12, NaCl을 함께 제외한 경우 배출속도는 대조군 수준에 미달된 데 비하여 0.2 mM Cac12, 10 mM NaCl첨가시에는 대조군의 180%였다. 아메바 수축포의 배출작용이 Na+이온 배출기구로 보고(Pottier efaf., 1987) 이들 결과를 종합해 볼때 아메바의 세포막에는 Na+ 이온의 투과수단으로 칼슘제거에 의해서 촉진확산되는 것과 Na+이온 농도증가에 따른 단순확산이 있을 것으로 사료된다.

• Restorative Dentistry and Endodontics
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• v.31 no.2
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• pp.119-124
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• 2006

The purpose of this study was to evaluate the effect of newly developed endodontic root canal cleanser (MTAD) on the apical leakage of obturated root canal using an electrochemical method. Canals of 60 extracted single-rooted human teeth were prepared by using a crown-down technique with rotary nickel-titanium files. In Group 1 (positive control group) and 2 (negative centre) group), 5.25% NaOCl was used as a canal irrigant and no canal wall treatment was done. In group 3 only 5.25% NaOCl were used as canal irrigant, canal wall treatment and final rinse. In group 4, specimens were irrigated with 5.25% NaOCl, treated with 5 ml of 17% EDTA for 5 minutes and final rinsed with 5.25% NaOCl Specimens of group 5 were irrigated with 1 3% NaOCl and treated with 5 ml of MTAD for 5 minutes. All root canals are dried with paper points and obtuated with gutta-percha and AH plus as a sealer using a continuous wave of condensation technique except in the group 1. The electrical resistance between the standard and experimental electrodes in canals was measured over a period of 10 days. Rising of apical leakage with time was observed for all the groups. Group 4 and 5 showed lower apical leakage than group 3 but differences between the group 3, 4 and 5 were no statistical significance at any measurement time.

• Journal of the Korean Chemical Society
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• v.40 no.1
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• pp.72-80
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• 1996

A chitinase-producing bacterium, Serratia marcescens JM, was isolated from a seashore muds. A chitinase was purified by ammonium sulfate precipitation, affinity adsorption, hydroxylapatite and sephadex G-200 column chromatography. The chitinase obtained from Serratia marcescens JM was purified 42.2 folds with the overall yield of 7.1%. The purified chitinase showed a single band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 59,000 and the apparent kinetic parameters $K_m\;and\;V_{max}$ for the purified chitinase were 5.17 mg/mL and 39.8 unit/mL, respectively. The optimum pH and temperature of the purified chitinase were 7.0 and 50$^{\circ}C$, respectively and the purified enzyme was stable on pH 7.0 up to 50$^{\circ}C$. The enzyme were activated by $Cu^{2+},\;Ca^{2+}\;and\;Mg^{2+}$ and inhibited by $Hg^{2+}$ respectively. In addition, Cysteine increased the chitinase activity and EDTA, MIA, PCMB and SDS inhibited enzyme activities. Major cations, $MG^{2+},\;Ca^{2+},\;K^+\;and\; Na^+$ present in seawater slightly stimulated the chitinase activity.

• Journal of the korean veterinary medical association
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• v.17 no.2
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• pp.63-71
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• 1981

Experimental hypocalcemia was induced in normal goats by intravenous administration with various concentration of $Na_2-EDTA$ solution. Tile results are summarized as follows: 1. Progressive depression of reflexes and body temperature, paresis,

• Journal of the korean veterinary medical association
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• v.17 no.6
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• pp.25-33
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• 1981

Changes in plasma calcium and inorganic phosphorus level, clinical signs and electrocardiogram in goats were observed during the induction of hypocalcemia (uhntil death) by the jugular intravenous infusion of 0.2M $Na_2-EDTA$ solution at a rate

• Korean Journal of Microbiology
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• v.37 no.1
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• pp.15-20
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• 2001

In this study, we have isolated bacterial cell wall lytic enzyme in the culture supernatant of Aspergillus sp. HCLF-4. This hydrolase showed cell wall lytic activity against Anabaena cylindrica. The extracellular enzyme was produced by Aspergillus sp. HCLF-4 when it was grown in a PDB media containing 0.05% heat killed Micrococcus luteus cells. The molecular weight of lytic enzyme was about 14.3 kDa. The optimal pH and temperature for the activity of this enzyme were 3.0~4.0 and $30^{\circ}C$, respectively. This hydrolase activity was reduced by $Na^{+}$, $Li^{+}$, $Ca^{2+}$, $Cu^{2+}$, $Fe^{3+}$, EDTA, and PMSF, whereas it was increased by $Mg^{2+}$, $Mn^{2+}$>. The enzyme has N-acetylmuramyl-L-amidase or endopeptidase activity.

• Journal of the Korean Chemical Society
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• v.33 no.6
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• pp.601-606
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• 1989

The effects of temperature and retaining ion on the separation factor (${\alpha}$) and distribution ratio (D) of some lanthanides ($Pr^{3+},\;Nd^{3+},\;Sm^{3+},\;and\;Er^{3+}$) have been studied in the EDTA solution as an elutant by using Amberite IR 120 + resin. The retaining ions on the resin were ${NH_4}^+,\;Na^+,\;K^+,\;Mg^{2+},\;Ca^{2+},\;Zn^{2+}$and $Ce^{3+}$. Separation factor of Nd/Pr is much improved by using $Ce^{3+}$ as retaining ion. The distribution ratios were decreased with the increase of temperature, but separation factors did not always increase with the increase of temperature. However, in the case of $Ce^{3+}$ as retaining ion, separation factors of Nd/Pr and Sm/Nd were increased with the increasing of temperature. And also in the case of $Zn^{2+}$ as retaining ion, separation factor of Er/Sm was increased with the increasing of temperature.

• Korean Journal of Environmental Agriculture
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• v.4 no.1
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• pp.25-30
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• 1985

In order to characterize relationship between accumulation of cadmium, zinc and lead in soil and soil chemical properties and also to choose a suitable soil extractant for the prediction model of heavy metal content in brown rice, four extractants-0.1 M HCl, 0.1 M $HNO_3$, 0.1 M $NH_4-oxalate$ and 0.001 M 2Na-EDTA, were compared by analyzing 84 soil samples collected from paddy fields adjacent to five zinc-minig sites. Contents of Cd, and Pb in soil increased with Zn content and those of three elements were found to be much higher in surface soil ($0{\sim}15 cm$) than suvsqrface soil ($15{\sim}30 cm$). Contents of these elements in soil were positively correlated with soil pH, but its correlation between extractable heavy metal content and organic matter or CEC varied from region to region. These three elements were negatively correlated with Mg content of soils. The extractability of the metals was in the order 0.1 M $HCI{\geq}0.1 M$ $HNO_3>0.001 M$ 2Na-EDTA>0.1 M $NH_4-oxalate$.

• Journal of the Korean Chemical Society
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• v.29 no.2
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• pp.137-143
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• 1985

Construction of a liquid membrane type of cupric ion selective electrode and its application to the potentiometric titration have been studied. A liquid ion-exchange membrance was prepared by extracting Cu(II) in aqueous solution into 1-(2-pyridylazo)-2-naphthol/nitrobenzene. A Ag/AgCl internal reference electrode was dipped into the aqueous reference solution of $1.00 {\times} 10^{-3}M\;Cu(NO_3)_2$ buffered with HAc-NaAc buffer solution, which was in contact with the nitrobenzene extract. The electrode showed the nernstian response to Cu(II) in the concentration range from $1.00{\times} 10^{-6}$ to $1.00{\times} 10^{-3}$M. The most suitable ion-exchanger concentration in the liquid membrane was $1.00{\times} 10^{-4}$M. The selectivity coefficients of the electrode for the various metal cations were investigated. The electrode was applied to the potentiometric titration of Cu(II) with EDTA.

• The Korean Journal of Mycology
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• v.33 no.2
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• pp.75-80
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• 2005

A carboxymethyl cellulase (CMCase) has been purified from Loweporus roseoalbus. The molecular weight of the purified CMCase was estimated to be 28.5 kDa by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The maximum activity of the purified CMCase was observed at pH 4.0 and $30^{\circ}C$, and stable for pH 3 to 5 to maintain 60% activity. The CMCase activity was activated by SDS and inhibited by PMSF and 1,10-phenanthroline. The enzyme activity was also decreased by the addition of ethylene diamine tetraacetic acid (EDTA), suggesting that the purified CMCase is metalloenzyme.