• Journal of Korean Society of Transportation
• /
• v.15 no.1
• /
• pp.129-156
• /
• 1997

8차로 고속도로에서 중앙분리대와 길 어깨에 의해 측방 여유폭이 제공되는 외측차 로(1.4차로)와 측방 여유폭이 제공되지 않는 내측차로 (2.3차로)에서 나타나는 운전자의 횡 방향 주행특성을 4개 지점에서 비디오 촬영하여 분석한 결과는 다음과 같다. (1) 차량의 횡 방향 주행궤적은 차로의 중심으로부터 주행방향의 좌측으로 이격된 주행 행태를 보이고 있 으며 이는 운전석의 위치에 의한 영향으로 판단된다. (2) 차량의 병행 주행시 외측 차로의 중심 이격 거리는 평균 0.38m이고 내측차로의 중심 이격 거리는 평균 0.34m로 나타났으며 T-test 겨로가 내측 차로와 외측 차로의 주행 이격 거리는 신뢰도 95%에서 상이한 것으로 나타났다. (3) 외측 차로의 주행궤적간 이격 거리는 평균 3.90m이고 내측 차로의 주행궤적 간 이격 거리는 평균 3.54m로서 내측 차로의 주행궤적간 이격 거리는 외측 차로의 주행궤 적간 이격 거리보다 0.36m 작다. 특히 내측 차로의 주행궤적간 이격 거리는 내측 차로간 차로 중심간 간격인 3.6m 보다 0.1m 작은 것으로 나타났다. (4) 내측차로 확장 대안으로 기존 도로폭 유지안 (3.5m, 3.7m, 3.5m)과 기존 도로폭 확장안 (3.6m, 3.7m, 3.7m, 3.6m)을 고려할 수 있으며 두 대안의 비교·분석결과 경제적 영향을 고려할 때 기존 도로폭 유지안이 우수한 것으로 분석되었다.

• Journal of Microbiology and Biotechnology
• /
• v.11 no.3
• /
• pp.452-457
• /
• 2001

The glutaryl 7-aminocephalosporanic acid (glutaryl 7-ACA) acylase was purified from Pseudomonas diminuta KAC-1 cells isolated from soil, and characterized. The acylase was purified by procedures including ammonium sulfate fractionation and column chromatographies on DEAE-Sepharose, Phenyl-Sepharose, Q-Sepharose, and Superose 12H/R. The negative acylase was found to be composed of two subunits with molecular masses of approximately 55 kDa and 17 kDa, respectively. The isoelectric point of the enzyme was 4.0. The specific activities of the purified acylase were 8.0 and 7.0 U/mg on glutaryl 7-ACA and glutaryl 7-aminodesacetoxy cephalosporanic acid (glutaryl 7-ADCA), respectively, and $K_m$ values were 0.45 mM for glutaryl 7-ADCA and 0.67 mM for glutaryl 7-ADCA. The enzyme had a pH optimum at 8.0 and a tmperature optimum at $40^{\circ}C$. The acylase catalyzed the synthesis of glutaryl 7-ACA from glutaric acid and 7-ACA as well as the hydrolysis of glutaryl 7-ADCA, although the reaction rate of the synthesis was slower than that of the hydrolysis. In addition, it was found that the enzyme had a glutaryl transferase activity, thereby transferring the glutaryl group from one cephalosporin nucleus to another.

• Microbiology and Biotechnology Letters
• /
• v.14 no.6
• /
• pp.441-446
• /
• 1986

Some properties of extracellular guanine deaminase produced by Pseudomonas synxantha A3 were studied. The enzyme was stable at pH 6.5-7.5 and generally stable when it was incubated at 4$0^{\circ}C$ for 10 minutes but inactivated gradually above 4$0^{\circ}C$. When the enzyme in 0.2M potassium phosphate (pH 8.0) was stored at room temperature, it was stable for thirty days. Alcohols and acetone were not effective for the eyzyme stability. The optimum pH and temperature for the enzyme activity were around pH 7.0-8.0 and 5$0^{\circ}C$, respectively. The enzyme was inhibited by 1mM of Hg$^{++}$, Ag$^+$ and Li$^+$ and by 0.1mM of Ag$^+$ with about 50% loss of activity. The enzyme inhibited by Li$^+$ was reactivated by EDTA. 1 mM of pentachlorophenol and p-CMB inactivated the enzyme with 50% and 40% loss of activity, respectively. The enzyme inactivated by p-CMB was reactivated by glutathione.

• Korean Journal of Environmental Agriculture
• /
• v.37 no.1
• /
• pp.21-27
• /
• 2018

BACKGROUND: Although 1 M $NH_4OAc$ (pH 7.0) is predominantly used as the extractant of exchangeable cations in agricultural soils, this method is unsuitable for extracting the cations in saline and calcareous soils. This study was performed to select a proper method to determine exchangeable cations in vinyl greenhouse soils. METHODS AND RESULTS: Exchangeable cations (Ca, Mg, K, Na) in saline vinyl greenhouse soils were determined after extraction with 1 M $NH_4OAc$ (pH 7.0 and 8.5) and 1 M alcoholic $NH_4Cl$ (pH 8.5). Sum of exchangeable cations of the soils extracted with 1 M $NH_4OAc$ at pH 7.0 was 1.9-2.5 times greater than soil cation exchange capaity determined at pH 7.0, even though soluble salts were pre-removed. A similar result was found when the cations were extracted with 1 M $NH_4OAc$ at pH 8.5. Those results are mostly due to the overestimation of exchangeable Ca and Mg, linked to a partial dissolution of sparingly soluble salts in $NH_4OAc$ solution. When extracted with 1 M alcoholic $NH_4Cl$ at pH 8.5, extractable Ca and Mg decreased significantly due to the lower solubility of Ca and Mg carbonates in the extractant. And the sum of exchangeable cations was very close to the corresponding exchange capacity of soils. CONCLUSION: Alcoholic $NH_4Cl$ (pH 8.5) is proposed as a reliable extractant in determination of exchangeable cations in saline vinyl greenhouse soils. And soluble salts should be removed prior to the extraction of exchangeable cations.

• Journal of Acupuncture Research
• /
• v.21 no.3
• /
• pp.107-119
• /
• 2004

Objective : The purpose of this study was to investigate the effect of Bee Venom and melittin on the lipopolysaccharide(LPS) and sodium nitroprusside(SNP)-induced expressions of Cell viability, nitric oxide(NO), inducible nitric oxide synthase(iNOS), extra-signal response kinase(ERK), jun N-terminal Kinase(JNK) and p38 kinase(p38)- mitogen activated protein kinase(MAPK) Family- in RAW 264.7 cells, a murine macrophage cell line. Methods : The expressions of cell viability by MTT assay, NO by Nitrite assay and iNOS, ERK, JNK and p38 were determined by Western blotting. Results : 1. Compared with the control group, 0.5, 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin increased cell viability of RAW 264.7 induced by LPS and SNP significantly respectively. 2. Compared with the control group, 0.5, 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin inhibited expression of NO induced by LPS and SNP significantly respectively. 3. Compared with the control group, 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin inhibited expression of iNOS induced by LPS significantly and 0.5, 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin inhibited expression of iNOS induced by SNP significantly. 4. Compared with the control group, the expression of ERK induced by LPS and SNP decreased significantly in the treatment groups of $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin, which of p-ERK by LPS also did in 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin, but which of p-ERK by SNP did not decrease. 5. Compared with the control group, the. expression of JNK induced by LPS and SNP decreased significantly in the treatment groups of 5, $10{\mu}g/m{\ell}$ melittin, which of p-JNK by LPS in 5, $10{\mu}g/m{\ell}$ melittin and by SNP in $1{\mu}g/m{\ell}$ bee venom and $10{\mu}g/m{\ell}$ melittin decreased significantly. 6. Compared with the control group, the expression of p38 induced by LPS did not have significant difference, which induced by SNP decreased significantly in the treatment groups of 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin. p-p38 induced by LPS decreased significantly in the treatment group of $10{\mu}g/m{\ell}$ of melittin, which induced by SNP also decreased significantly in 0.5, 1, $5{\mu}g/m{\ell}$ bee venom and 5, $10{\mu}g/m{\ell}$ melittin.

• Korean Journal of Microbiology
• /
• v.30 no.4
• /
• pp.239-245
• /
• 1992

Buci1llr.s 11c~h~n~1rnSiSi.As 3-2MI which is responsible for the special taste of traditionalKorean soy sause produced two kinds of proteinase. The activity of the proteinasc I washigher about two fold than that of proteinase 11. The optimai, reaction pH of proteinaseI and I1 wcre found to be 7-1 1.5 and 7-9. respectively. Proteinase I1 was more stable andactive than proteinase I at pH ranges around 3 to 5. The optimal te~tlperature of proteinaseI and I1 were 502. The temperature stabilitl of proteinase I1 was Inore stable thanproteinase 1 at temperature range around 30-quot;~A. ctivities of proteinase I and I1 graduallydeclined above $30^{\circ}$C and 45C. respectively. Proteinasc 1 was more active than proteinaseI1 at salt concentration range around 25-3500. The K,,, values of casein and soy proteinfor proteinase I were 6.89 mglml and 3.98 mglml. In case of proteinase 11. they were 9.00mgiml anti 11.44 111g/ml. respectively. The activity of the crudc enzyme was increased by1 rnM Pb(CH3COO). but was decreased by 5 n1M and 10 rnM of HgS04 and ZnS04. Thetwo proteinases produced amino acids and peptides from the soybean protein. The peptideswere digested into amino acids. Both protcinases were found to be the main enzymes thatproduced amino acids which make the main taste of traditional Korean soy sauce.al Korean soy sauce.

• Journal of the Korean Chemical Society
• /
• v.53 no.1
• /
• pp.90-94
• /
• 2009

• The Korean Journal of Pesticide Science
• /
• v.6 no.1
• /
• pp.31-35
• /
• 2002

Objectives of this study were to determine if impurities in technical grade benfuracarb inhibit glutathione-S-transferase and amidase and to identify structures of impurities in technical grade benfuracarb. Technical grade benfuracarb, active ingredient, and impurity inhibited glutathione-S-transferase, and their $I_{50}$ were $9.7{\times}10^{-4}M,\;>1.0{\times}10^{-3}M,\;1.8{\times}10^{-4}M$, respectively. Such inhibition, however, was not higher than that by ethacrynic acid, a selective inhibitor to GST. Technical grade benfuracarb, active ingredient, and impurity also inhibited amidase, and their $I_{50}$ were $6.0{\times}10^{-5}M,\;4.3{\times}10^{-4}M,\;7.6{\times}10^{-5}M$, respectively. Our results show that the inhibition of both detoxifying enzymes by impurities in benfuracarb was 10-fold lower than that by active ingredient, suggesting that both active ingredient and impurities are involved in the inhibition of both detoxifying enzymes. Of four impurities (IM $1{\sim}4$) that were separated from technical grade benfuracarb, IM 2 and IM 3 inhibited GST and amidase. Based on data from IR, $^1H$-NMR, $^{13}C$-NMR and MS, it was determined that IM 2 is ethyl-N-isopropylamino propionate and IM 3 is ethyl-N-isopropyl-N(chlorosulfenyl)aminopropionate.

• Journal of the Korean Institute of Illuminating and Electrical Installation Engineers
• /
• v.15 no.1
• /
• pp.118-124
• /
• 2001

To guide the esti-on of electric d e d and energy saving, this proposed the Power Laaddensity, Elechic pwer consumption and the installed state of Power facility. For this purp~se, it wasconducted a questionnaire survey of the consumption-cattern of Electric power in 1W a p a r t t housings.As a 1-esult it is found that (i) the d m u m value of Power Load density is 7.70[~A/m"l, (ii) the avtragevalue of Power Load dens'||'&'||' is ~ . ~ A / mm' dl (iiijthe average load rate is Ed[%]. Also, the consumptionof electricity one year at tlie whole a m n t s of couniry is 14,0X[GWyearl, it was equivalent to 7[%1 ofthe total-consunmhon of electricity one year at the whole of co1mtnr. co1mtnr.

• Journal of Embryo Transfer
• /
• v.29 no.4
• /
• pp.385-391
• /
• 2014

Objective of this study was to investigate the effect of nicotinic acid (NA) on the characteristics in fresh semen of miniature pig. We evaluated viability, acrosome reaction and mitochondrial integrity of sperm on 0, 3, 7 and 10 days during storage period with nicotinic acid. As results, the survival rate of sperm in 15 mM NA (day 3, $87.8{\pm}1.2%$; day 5, $84.0{\pm}2.7%$; day 7, $82.2{\pm}0.9%$) and 30 mM NA (day 3, $87.7{\pm}0.3%$; day 5, $84.4{\pm}2.5%$; day 7, $82.3{\pm}0.7%$) groups were higher than control and 5 mM NA groups in 3, 7 and 10 days of semen storage. The NA-treated sperm on 10 day was used day for observing acrosome integrity. The survival sperm with acrosome reaction was higher in 30 mM NA group (day 3, $2.7{\pm}0.2%$; day 5, $3.3{\pm}0.6%$; day 7, $11.4{\pm}0.3%$) than in the control, significantly (P<0.05). Moreover, the live sperm with mitochondrial integrity was higher in whole treatment groups of NA than control group, significantly (P<0.05). Specially, most mitochondrial integrity on 10 day of semen storage was significantly higher in 30 mM NA group ($90.2{\pm}1.6%$) than other treatment groups (control, $81.8{\pm}3.1%$; 5 mM NA, $83.4{\pm}3.0%$; 15 mM NA, $89.1{\pm}0.7%$, P<0.05). In conclusion, supplement of NA in liquid semen of miniature pig can improve and maintain semen quality, such as viability, acrosome reaction, and mitochondria integrity.