Special Theme_재난통신 및 방송 - 국가통합지휘무선통신망 구축 현황 및 계획

정안식,Jeong, An-Sik 한국정보통신기술협회 2010 TTA저널 Vol.131 No.-

밥상의 새로운 발견 - 마늘

정안식,Jeong, An-Sik 대한산업안전협회 2007 안전기술 Vol.117 No.-

개선된 공간벡터형 히스테리시스 전류제어기법

정안식(An Ski Jeong),박기원(Ki Won Park),정승기(Seung Gi Jeong) 대한전기학회 1999 대한전기학회 학술대회 논문집 Vol.1999 No.7

셀레나움을 투여한 백서에 간에 있어 glutathione S - transferase 의 유도

박영일,정안식 ( Young Yil Bark,An Sik Chung ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.1

The effect of sodium selenites (Na₂SeO₃, Se) on the activities of glutathione (GSH) S-transferase was examined. The treatment of rats with Se(5,10 and 20μmoles) caused dose-dependent increase in the activities of GSH S-transferases in male rats. Furthermore, repeated sodium selenite administration increased the activities of GSH S-transferases in male and female rats. GSH S-transferases are a dimer and composed of Ya, Yb (or Yb`) and Yc subunits. Se treatment elevated the relative amount of Yb (Yb`) subunits in both sexes. The increaments of Yb (Yb`) subunits were from 29.5% to 46.4% in male rats and from 4.8% to 9.3% in female rats. The separation of GSH S-transferases into basic and neutral/acidic ones was performed using the method of chromatofocusing. Six peaks of enzymes correspond to fractions of isozymes L₂, BL, B₂, A₂, AC and C₂ by the order of chromatofocusing elution. The administration of Se in male and female rats induced, basic transferases, A₂ and C₂ isozymes but not AC isozymes. C₂ isozyme increased 7.72 fold in males and 2.72 fold in females, and A₂ isozyme increased 1.56 fold and 2.04 fold, respectively. Selenium treatment also increased activity of neutral/acidic isozymes 1.37 fold in male but did not increased the activity of neutral/acidic isozymes in female. The significant differences between male and female rats by Se administration were C₂ isozymes and neutral/acidic GSH S-transferases.

색소에 접합된 $\beta$-glucan을 이용한 $\beta$-glucan 분해효소 생산 균주의 분리 및 동정

양진오,정안식,이성택 한국미생물학회 1987 미생물학회지 Vol.25 No.4

A bacterium K-4-3, producing $\beta$-glucan hydrolyzing enzyme, was isolated from soil and identified to be Bacillus subtilis by its morpholohical and physiological characteristics. $\beta$-glucan was coloured using cibacron blue 3G-A and cross linded by the addition of 1, 4-butanedioldiglycidyl ether. This substrate was used for the isolation of $\beta$-glucanase producing microorganism. The $\beta$-glucan hydrolyzing enzyme actibity from isolated K-4-3 strain was also measured using the modified substrate. Bacillus subtilis K-4-3 produced the highest extracellular $\beta$-glucan hydrolyzing activity in the basal medium containing $\beta$-glucan as a carbon source, peptone and tryptone as a nitrogen source, and magnesium sulfate as an inorganic salt. The optimum temperature and initial pH for $\beta$-glucanase production by Bacillus subtilis K-4-3 were $37^{\circ}C$ and pH6. The highest enzyme activity was obtained at the culture age of 54 hrs with rotary shaking at $37^{\circ}C$. The crude enzyme showed the highest activity at pH 7.5-8.0 and $65^{\circ}C$.

Induction of some Glutathione S-transferases in rat liver by selenium

박영일,정안식,Bark, Young-Yil,Chung, An-Sik 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.1

소디움 셀레나이트 $Na_2SeO_3$를 쥐에 투여하였을 때 Glutathione S-transferase의 활성도에 미치는 영향을 조사했다. 셀레니움 농도를 각기 달리하여 5, 10 그리고 $20{\mu}mol$ 농도로 숫쥐에 주사했을 때, GSH S-transferase의 활성도는 투여된 셀레니움의 양에 따라 증가했으며, 반복해서 소량의 소디움 셀레나이트를 소량으로 계속 주사했을 시에 숫쥐와 암쥐에 있어 GSH S-transferase의 활성도가 또한 증가하였다. GSH S-transferase는 dimer이며, 그 단위는 Ya, Yb (또는 Yb') 그리고 Yc로 이루어져 한다. 셀레니움을 투여했을 때 암쥐, 숫쥐 모두 Yb(Yb') 단위가 증가했다. Yb 단위 증가량은 숫쥐의 경우 29.5%에서 46.4%, 암쥐의 경우 4.8%에서 9.3% 정도이다. GSH S-transferase의 분리는 Chromatofocusing 방법에 의해 분리했다. 염기성 효소의 여섯개 peak는 Chromatofocusing elution 순서에 의해 $L_2$, BL, $B_2$, $A_2$, AC와 $C_2$인 동위효소와 상응한다. 암쥐와 숫쥐에 셀레니움을 투여했을 때 염기성 transferase인 $A_2$와 $C_2$ 동위효소 (isozyme)는 유도되었으나 AC 동위효소 (isozyme)는 유도되지 않았다. $C_2$ 동위효소는 숫쥐의 경우 7.72배 증가했으며, 암쥐의 경우 2.72배 증가했다. 그리고 $A_2$ 동위효소는 숫쥐의 경우 1.56배 증가했으며, 암쥐의 경우 2.04배 증가했다. 또한 셀레니움 투여시 숫쥐의 경우 neutral/acidic 동위효소 1.37배 활성도가 증가했으나 암쥐의 경우 증가하지 않았다. 셀레니움 투여량에 의한 숫쥐와 암쥐간의 유의적인 차이점은 $C_2$ 동위효소와 neutral/acidic GSH S-transferase에서 나타냈다. The effect of sodium selenites ($Na_2SeO_3$, Se) on the activities of glutathione (GSH) S-transferase was examined. The treatment of rats with Se(5,10 and $20{\mu}moles$) caused dose-dependent increase in the activities of GSH S-transferases in male rats. Furthermore, repeated sodium selenite administration increased the activities of GSH S-transferases in male and female rats. GSH S-transferases are a dimer and composed of Ya, Yb (or Yb') and Yc subunits, Se treatment elevated the relative amount of Yb (Yb') subunits in both sexes. The increaments of Yb (Yb') subunits were from 29.5% to 46.4% in male rats and from 4.8% to 9.3% in female rats. The separation of GSH S-transferases into basic and neutral/acidic ones was performed using the method of chromatofocusing. Six peaks of enzymes correspond to fractions of isozymes $L_2$, BL, $B_2$, $A_2$, AC and $C_2$ by the order of chromatofocusing elution. The administration of Se in male and female rats induced, basic transferases, $A_2$ and $C_2$ isozymes but not AC isozymes. $C_2$ isozyme increased 7.72 fold in males and 2.72 fold in females, and $A_2$ isozyme increased 1.56 fold and 2.04 fold, respectively. Selenium treatment also increased activity of neutral/acidic isozymes 1.37 fold in male but did not increased the activity of neutral/acidic isozymes in female. The significant differences between male and female rats by Se administration were $C_2$ isozymes and neutraVacidic GSH S-transferases.

EFFECT OF SELENIUM ON DIFFERENCE IN THE ACTIVITIES OF ISOZYMES OF HEPATIC GLUTATHIONE - S - TRANSFERASE IN RATS

박영일,정안식 한국생화학분자생물학회 (구 한국생화학회) 1987 추계학술대회집 Vol.- No.-

폐 게껍질을 이용한 중금속 흡착특성

이성홍,박상원,정안식 대한환경공학회 1992 대한환경공학회 학술발표논문집 Vol.1992 No.12

색소기질을 이용한 Bacillus subtilis의 $\beta$-glucanase 정제

이성택,양진오,정안식 한국미생물학회 1988 미생물학회지 Vol.26 No.3

토양에서 분리 동정한 Bacillus subtilis K-4-3를 $\beta$-glucanase생산을 위하여 발효조를 사용한 결과 flask내 배양보다 배양 시간을 단축하였고 높은 역가의 조효소액을 얻을 수 있었다. 배양여액으로부터 균체의 $\beta$-glucanase는 색소에 접합된 변형기질을 이용하여 ammonium sulfate, fractionation Sephadex G-100 gel filtration, DEAE-Sphacel ion exchange chromotography의 순으로 정제하였으며, 정제효소는 15배로 정제되어 비활성이 25.7 unit/mg이였으며, 수율은 4.2%이였다. 본 효소의 일반적 특성을 검토한 결과 정제효소는 $50^{\circ}C$에서 최적반응을 나타내었고 그 활성은 $50^{\circ}C$에서 30분간 열처리에도 안정하였다. 효소의 최적 pH는 7.0 부근이었고 금속이온의 영향으로는 $Fe^{3+}$에 의해 강하게 저해받았고 $Li^{+1}$에 의해 약간 활성화 되였다. 분자량은 SDS 전기영동에 의해 17,000.으로 추정되었으며 monomer였다. 또한 본 효소에 의한 분해산불을 TLC로 관찰한 결과 2탄당, 3탄당 빛 4탄당으로 추정되는 분해산물을 얻을 수 았었으나 최종산물인 glucose는 얻을 수 없었다. Bacillus subtilis K-4-3, which produces considerable amount of $\beta$-glucanase was selected among extracellular $\beta$-glucanase-producing bacteria isolated from soil. $\beta$-glucanase was purified by ammonium sulfate fractionation, Sephadex G-100 gel filtration and DEAE-sephacel ion exchange chromatography. The purified enzyme revealed a single band by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 17000 dalton by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature of the purified $\beta$-glucanase were 7.0 and $50^{\circ}C$, respectively. The enzyme was strongly inhibited by 1.0mM of $Fe^{3+}$, and activated by 1.0mm of $Li^{}47+$. The absence of glucose after thin layer chromatography of reaction products revealed that the purified enzyme contains no cellobiase or laminarinbiase activity. The loberation of ki, tri-and tetra-saccharide as reaction products can be explained by endoaction of the enzyme.

Induction Pattern of Glutathione S-transferase Isozymes in Rat Liver by Administration of 2(3)-tert-butyl-4-hydroxyanisole: A Possible Relationship between Isozyme and Glutathione Peroxidase

남상례,변부형,정안식,Nam, Sang-Rae,Byun, Boo-Hyung,Chung, An-Sik 생화학분자생물학회 1990 한국생화학회지 Vol.23 No.2

항암의 기작과 독성 효과를 지닌 2(3)-tert-butyl-4-hydroxyanisole(BHA)가 백서의 간과 다른 조직에서 해독하는 효소를 유도하는 것으로 생각한다. 본 연구는 BHA가 백서의 간에서 gluthathione S-transferase의 specificisozymes을 유도하는지를 알기위해 실험했다. 백서의 먹이에다 0.75% BHA를 첨가하여 3일 동안 투여했을 때, 간세포질의 glutathione, GSHS-transferase 및 glutathione reductase의 농도는 증가했다. 반대로, GSH peroxidase의 활성은 BHA 투여에 의해 감소했다. 특히, GSH S-transferase의 $L_2$와 $A_2$ 염기성 동위효소는 BHA 투여에 의해 각각 1.35와 1.50배로 유의적으로 유도되었으며 $B_2$, AC와 $C_2$ 동위효소는 거의 8내지 12% 이상 유도되었다. 그러나 neutral/acidic GSH S-transferase의 동위효소는 0.37배 유의적으로 감소됐으며 BL 동위원소는 BHA 투영에 의해 약 0.90배 감소됐다. $L_2$, BL, $B_2$ 및 $C_2$의 selenium-dependent glutathione peroxidase의 활성을 각각 1.46, 1.53, 1.19 그리고 1.61배 증가되었다. Selenium-independent peroxidase는 $L_2$2 동위 효소를 제외하고는 Selenium-dependent peroxidase와 유사한 형태를 나타냈는데, 처리한 군과 처리하지 않은 군간의 활성은 아무런 차이가 없었다. $L_2$, BL 그리고 $B_2$의 동위효소는 Selenium-independent peroxidase의 활성에 비해 Selenim-dependent peroxidase의 활성의 2배 내지 3배 더 높음을 나타냈다. 그러나, $A_2$, AC 및 $C_2$ 동위효소는 Se-dependent peroxidase의 활성에 비해 Se-independent peroxidase의 활성이 수배 이상을 나타냈다. The mechanism by which 2(3)-tert-butyl-4-hydroxyanisole exerts anticarcinogenic and toxic effect in animals including human is believed to be the induction of detoxifying enzymes in the liver and other tissues. This study was designed to determine specific isozymes of glutathione S-transferase induced in rat liver by BHA. Administration of 0.75% BHA in diet for three days increased the concentration of glutathione and the activities of GSH S-transferase and of glutathione reductase in liver cytosol, while the activity of glutathione peroxidase was decreased by BHA treatment. Basic isozymes of GSH S-transferase $L_2$ and $A_2$ were induced significantly 1.35 and 1.50 fold, respectively by BHA administration. $B_2$, AC and $C_2$ isozymes were induced slightly more (8-12%)compared to the control group. But neutral/acidic isozymes of GSH S-transferase were reduced significantly 0.37 fold and BL isozyme was reduced slightly 0.90 fold by BHA administration. The activities of selenium-dependent glutathione peroxidase of $L_2$, BL, $B_2$ and $C_2$ was increased 1.46, 1.53, 1.19 and 1.61 fold, respectively. Selenium-independent peroxidase showed similar patterns of Se-dependent peroxidase except $L_2$ isozyme, that showed no difference between treated vs nontreated. Isozymes $L_2$, BL and $B_2$ showed 2-3 times-higher activities of Se-dependent peroxidase than those of Se-independent peroxidase but $A_2$, AC and $C_2$ isozyme revealed several folds more activities of Se-independent peroxidase than those of Se-dependent peroxidase.