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오리의 Uropygial Gland 로부터 Malic Enzyme 의 정제 및 그 특성
박완제,김유삼 ( Wan Je Park,Yu Sam Kim ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.1
Malic enzyme from the uropygial gland of duck was purified by the combination of 2`,5`-ADP agarose and DEAF-Sephacel in the electrophoretically homogeneous form. Purification fold and specific activity were 183 and 174 unit/㎎ protein, respectively. Molecular size of subunit determined by SDS-polyacrylamide gel electrophoresis was 60, 000 dalton. Optimal pH was 7, 5 and Mn^(++) or Mg^(++) was required for activity. For the enzyme in uropygial gland the apparent Km for malate and NADP+ were 370μM and 10. 6μM respectively. In case of liver enzyme apparent Km for malate and NADP^+ were 606μM and 20.8μM, respectively. In uropygial gland and liver, the following product inhibition patterns were observed with malate and NADP^+ as variable substrates: NADPH, noncompetitive (Ki_G, 166μM; Ki_L, 97μM) and competitive (Ki_G, 43μM; Ki_L, 22μM) : pyruvate, uncompetitive (Ki_G, 26mM; Ki_L, 11mM) and uncompetitive (Ki_G, 32mM; Ki_L, 20mM) : bicarbonate, noncompetitive (Ki_G, 112mM; Ki_L, 36mM) and noncompetitive (Ki_G, 183mM; Ki_L, 63mM) . In addition to this kinetic difference between the enzymes from the gland and liver, electrophoretic mobility of the gland enzyme was also different from that of the liver enzyme, suggesting that these enzymes are isozymes each other and the gland enzymes are specially designed to meet the spcialized function of the unopygial gland.
Purification and Properties of Malic Enzyme from the Uropygial Gland of Peking Duck.
박완제,김유삼,Park, Wan-Je,Kim, Yu-Sam 생화학분자생물학회 1984 한국생화학회지 Vol.17 No.1
Uropygial gland에 있는 malic enzyme을 2',5'-ADP agarose affinity chromatography, DEAE-Sephacel ion exchange chromatography에 의해서 183배 정제하였으며 specific activity는 174 unit/mg protein이었다. 이렇게 정제된 효소는 SDS-polyacrylamide gel electrophoresis를 하였을 때 95% 이상의 순도를 나타냈으며, subunit의 분자크기는 약 60,000dalton이었다. 최적 pH는 7.5이었으며 이 효소의 활성을 나타내는데는 $Mn^{++}$이나 $Mg^{++}$ 이온이 필요하였다. Uropygial gland malic enzyme의 경우에 있어서 malate와 $NADP^+$에 대한 Km은 각각 $370{\mu}M$, $10.6{\mu}M$ 이었으며, liver malic enzyme의 경우는 $606{\mu}M$, $20.8{\mu}M$이었다. Uropygial gland와 liver 효소에 대한 product inhibition pattern은 서로 같은 양상을 나타나는데 즉, bicarbonate는 malate와 $NADP^+$에 대하여 모두 uncompetitive inhibitor이었고, pyruvate에 대하여서는 두 기질 모두 uncompetitive inhibitor이었으며, NADPH는 malate에 대하여 noncompetitive inhibitor이었으나 $NADP^+$에 대해서는 competitive inhibitor이었다. 그러나 uropygial gland 효소의 product (bicarbonate, pyruvate, NADPH)에 대한 Ki 값은 liver 효소의 Ki 값보다 2-3배정도의 높은 값을 나타냈다. Initial velocity plot과 produt inhibition pattern을 조사해본 결과 효소에 $NADP^+$가 먼저 결합한 후 다음에 malate가 들어와서 결합하게 되면 생성물이 $CO_2$, pyruvate, NADPH 순서로 유리되는 ordered kinetic mechanism을 갖는다는 사실을 알아 내었다. Uropygial gland에서 분리한 malic enzyme은 간에서 분리한 같은 효소에 대하여 이상과 같은 차이점이 있음은 물론 전기이동에 의하여서도 이동거리가 서로 다른 것으로 보아 하나의 isozyme인 것으로 예측되며 uropygial gland의 특별한 역할에 잘 맞도록 구성된 것으로 믿어진다. Malic enzyme from the uropygial gland of duck was purified by the combination of 2',5'-ADP agarose and DEAE-Sephacel in the electrophoretically homogeneous form. Purification fold and specific activity were 183 and 174 unit/mg protein, respectively. Molecular size of subunit determined by SDS-polyacrylamide gel electrophoresis was 60,000 dalton. Optimal pH was 7.5 and $Mn^{++}$ or $Mg^{++}$ was required for activity. For the enzyme in uropygial gland the apparent Km for malate and $NADP^+$ were $370{\mu}M$ and $10.6{\mu}M$ respectively. In case of liver enzyme apparent Km for malate and $NADP^+$ were $606{\mu}M$ and $20.8{\mu}M$, respectively. In uropygial gland and liver, the following product inhibition patterns were observed with malate and $NADP^+$ as variable substrates: NADPH, noncompetitive ($Ki_G$, $166{\mu}M$; $Ki_L$, $97{\mu}M$) and competitive($Ki_G$, $43{\mu}M$; $Ki_L$, $22{\mu}M$): pyruvate, uncompetitive($Ki_G$, $26{\mu}M$; $Ki_L$, $11{\mu}M$) and uncompetitive ($Ki_G$, $32{\mu}M$; $Ki_L$, $20{\mu}M$): bicarbonate, noncompetitive ($Ki_G$, $112{\mu}M$; $Ki_L$, $36{\mu}M$) and noncompetitive ($Ki_G$, $183{\mu}M$; $Ki_L$, $63{\mu}M$). In addition to this kinetic difference between the enzymes from the gland and liver, electrophoretic mobility of the gland enzyme was also different from that of the liver enzyme, suggesting that these enzymes are isozymes each other and the gland enzymes are specially designed to meet the spcialized function of the unopygial gland.
Vibrio vulnipcus 에 대한 경구용백신 CJ-50002 의 일반약리작용
박완제(Wan Je Park),김영훈(Young Hoon Kim),정성목(Seong Mok Jeong),이영수(Young Soo Lee),신재규(Jae Kyu Shin),최재묵(Jae Mook Choi),이나경(Na Gyong Lee),이윤하(Youn Ha Lee) 한국응용약물학회 1999 Biomolecules & Therapeutics(구 응용약물학회지) Vol.7 No.1
CJ-50002 is an oral vaccine against V. vulnificus infection composed of whole cell lysate of V. vulnificus. The general pharmacological properties of CJ-50002 were evaluated in various animals and in vitro system. CJ-50002 at oral doses of 0.2, 2 and 20 mg/kg had no effect on general behavior in mice, chemoand electro-convulsions in mice, writhing syndrome induced by acetic acid in mice, body temperature in rats, charcoal meal propulsion in mice and urine and electrolytes excretion in rats. However, oral administration of CJ-50002 at dose of 20 mg/kg prolonged the hexobarbital-inuced sleeping inducing time in mice. In anesthetized dogs, CJ-50002 showed no effect on blood pressure, heart rate and ECG but decreased the respiratory rate and femoral blood flow at dose of 20 mg/kg. p.o. CJ-50002 had no effect on the contractile response of the isolated guinea pig ileum to various spasmogen at concentrations of 0.2, 2 and 20 ㎍/ml, respectively. Since these pharmacological effects of CJ-50002 were observed at dose much greater than those in clinical use (approximately 0.16 mg/kg, p.o.), it is likely that this vaccine may be relatively free of undesirable effects in clinical practice.
지르코늄 기반 유무기 복합다공체를 이용한 고압에서 SF6의 흡착 분리
김민범,박완제,김태훈,윤태웅,강조홍,김정훈,배윤상 한국공업화학회 2018 한국공업화학회 연구논문 초록집 Vol.2018 No.0
육불화황(SF<sub>6</sub>)은 주로 전력산업에서 많이 이용되며 사용 후 N<sub>2</sub>와 혼합물 형태로 대기 중으로 배출되어 SF<sub>6</sub>/N<sub>2</sub> 혼합물에서 SF<sub>6</sub>만을 선택적으로 분리하는 기술이 필요한데, 흡착을 이용한 분리는 에너지 소모가 적고 부산물을 만들지 않는다는 점에서 각광받고 있다. 압력순환식 흡착(PSA) 공정 적용을 위해서는 고압에서 좋은 SF<sub>6</sub>/N<sub>2</sub> 선택도의 흡착제 개발이 매우 중요하지만 현재까지 보고된 유무기 복합체(Metal-Organic Framework)들은 고압으로 갈수록 점점 낮은 SF<sub>6</sub> 선택성을 보인다. 따라서 본 연구에서는 큰 비표면적과 큰 기공을 가지며 수열안정성이 우수한 지르코늄 기반의 흡착제를 합성하였고, 기존 흡착제 대비 고압에서(~10기압) 우수한 SF<sub>6</sub> 선택성과 흡착용량을 확인하였다. ** This work was supported (in part) by the National Research Foundation of Korea under Grant (NRF-2016R1A2B4014256). Also, this work was supported by “Next Generation Carbon Upcycling Project” (Project No. 2017M1A2A2043449) through the National Research Foundation (NRF) funded by the Ministry of Science and ICT, Republic of Korea.