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문신철 세계기독교통일신령협회 2004 統一世界 Vol.- No.2
할아버지 할머니, 저 신철이에요. 막상 이렇게 카드를 쓰니 무엇부터 말씀드려야 할지 잘 생각이 안나네요. ‘만수무강 하세요’ 라든지 뭐 그렇게 얘기는 하지만 막상 저희들을 정말 편하게, 터놓고 말씀드린 적은 없는 것 같습니다.
이중 풍선 소장 내시경으로 진단한 와파린에 의한 소장 벽내 혈종
임동휘 ( Dong Hwi Rim ),은창수 ( Chang Soo Eun ),문신제 ( Shin Jae Moon ),배중호 ( Jung Ho Bae ),김태엽 ( Tae Yeob Kim ),이항락 ( Hang Lak Lee ),손주현 ( Joo Hyun Sohn ),전용철 ( Yong Cheol Jeon ),한동수 ( Dong Soo Han ) 대한장연구학회 2011 Intestinal Research Vol.9 No.2
Although bleeding is a major complication of oral anticoagulant therapy, warfarin-induced spontaneous intramural hematoma of the small bowel is a very rare complication. The clinical features of spontaneous intramural hematoma vary from mild abdominal pain to panperitonitis due to bowel perforation. Because spontaneous intramural hematoma can proceed to a life threatening situation, early diagnosis is of vital importance. Although there are a number of radiologic diagnostic tools available including abdominal ultrasonography and computed tomography, confirmation of the diagnosis through direct visualization of the involved bowel mucosa is very helpful. Direct confirmation of warfarin-induced spontaneous intramural hematoma of the small bowel is possible using double-balloon enteroscopy. We report a case of warfarin-induced spontaneous intramural hematoma with a review of the relevant literature. (Intest Res 2011;9:162-165)
ICR종 생쥐의 간에서 얻은 δ - Aminolevulinate Dehydratase 동위효소의 생화학적 성상
김문신,정규철 ( Moon Shin Kim,Kyou Chull Chung ) 생화학분자생물학회 1979 BMB Reports Vol.12 No.4
Two different fractions with δ-aminolevulinate dehydratase activity designated isozyme I and I[ tentatively were isolated from liver homogenate of ICR inbred mice by slightly modifying the procedure of Doyle and Schimke, and further their physicochemical properties were characterized as follows. 1. Optimal activities of the isozyme I and II appeared to be pH 6.5 in phosphate buffer. However, catalytic activities of the both isozymes were shown to be more active in Tris-HCl buffer at pH 7.5 than in the phosphate buffer at the same pH. 2. Both of the isozymes were found to be relatively heat stable, of which stability of the isozyme I was more resistant comparable to isozyme II. 3. Apparent Michaelis-Menten Constants of the both isozyme I and II in the present experiment were 2.1 × 10^(-4)M and 5.5 × 10^(-4)M, respectively. 4. Inhibition of the enzyme activity by heavy metals such as Pb^(++) and Hg^(++)+ in vitro was more debiliated in isozyme II than in isozyme I. 5. It was found that isozyme I could not be isolated by the same procedure as was done in the normal group from lead nitrate-treated group. In addition, the enzymatic activity of isozyme II was also decreased remarkably by the same treatment. The animals used have been treated by injecting intraperitoneally 1% lead nitrate solution with 1.3 ml/100 gm of body weight to each mouse 3 weeks prior to performing the experiment. 6. Both the isozyme I and II showed the different electrophoretic mobilities on immunoelectrophoresis. Rabbit anti-sera to isozyme II have been applied.
ICR 종 생쥐의 간에서 얻은 $\delta$-Aminolevulinate Dehydratase 동위효소의 생화학적 성상
김문신,정규철,Kim, Moon-Shin,Chung, Kyou-Chull 생화학분자생물학회 1979 한국생화학회지 Vol.12 No.4
ICR 종 친근교배계의 성숙한 생쥐 125마리에서 적출한 128.8gm의 간에서 Doyle and Schimke(1969)의 방법의 변법으로 $\delta$-ALAD를 분리정제하였던 바 분자량이 다른 2개의 효소분획을 얻었다(이 영원과 정 규철, 1979). 이 효소분획 I과 효소분획 II의 물리화학적, 효소화학적 및 면적화학적 성상을 조사하여 다음과 같은 결과를 얻었다. 1. Potassium phosphate 완충액에서의 두 효소분획의 최적 pH는 6.5로서 서로 같았으며, pH가 6.5이상으로 됨에 띠라 효소활성치는 계속 감소하였다. 그러나 pH7.5에서는 potassium phosphate 완충액을 사용할 때보다 Tris 완충액을 사용할 때 그 활성치가 높게 나타났다. 2. $\delta$-ALAD는 열에 대한 안정성이 비교적 강한 효소임을 알 수 있으며, 특히 효소분획 I의 안정성이 효소분획 II의 안정성보다 강하였다. 3. Michaelis-Menten 상수는 효소분획 I이 $2.1{\times}10^{-4}M$이고, 효소분획 II의 Km 값인 $5.5{\times}10^{-4}M$의 1/2.6이었다. 4. $Pb^{++}$ 및 $Hg^{++}$ 등 중금속에 의한 시험관내에서의 효소활성의 억제착용은 효소분획 I 보다는 효소분획 II에서 현저하였다. 5.1% lead nitrate 용액을 체중 100gm 당 1.3ml씩 생쥐의 복강내에 주사하고 3주 후에 간의 $\delta$-ALAD를 정제하였던 바 효소분획 I의 활성치는 완전히 없어졌고 효소분획 II의 활성치도 현저하게 감소하였다. 6. 효소분획 II에 특이한 토끼의 항혈청에 대한 효소분획 I과 효소분획 II의 면역화학적 반응을 보면 두 효소품획의 면역침전물의 이동양상은 서로 상이하였다. 이상의 연구 결과로 미루어 ICR종 생쥐의 $\delta$-ALAD에는 두 개의 동위효소가 있음을 알 수 있다. Two different fractions with $\delta$-aminolevulinate dehydratase activity designated isozyme I and II tentatively were isolated from liver homogenate of ICR inbred mice by slightly modifying the procedure of Doyle and Schimke, and further their physicochemical properties were characterized as follows. 1. Optimal activities of the isozyme I and II appeared to be pH 6.5 in phosphate buffer. However, catalytic activities of the both isozymes were shown to be more active in Tris-HCl buffer at pH 7.5 than in the phosphate buffer at the same pH. 2. Both of the isozymes were found to be relatively heat stable, of which stability of the isozyme I was more resistant comparable to isozyme II. 3. Apparent Michaelis-Menten Constants of the both isozyme I and II in the present experiment were $2.1{\times}10^-4M$ and $5.5{\times}10^-4M$, respectively. 4. Inhibition of the enzyme activity by heavy metals such as $Pb^{++}$ and $Hg^{++}$ in vitro was more debiliated in isozyme II than in isozyme I. 5. It was found that isozyme I could not be isolated by the same procedure as was done in the normal group from lead nitrate-treated group. In addition, the enzymatic activity of isozyme II was also decreased remarkably by the same treatment. The animals used have been treated by injecting intraperitoneally 1% lead nitrate solution with 1.3 ml/100 gm of body weight to each mouse 3 weeks prior to performing the experiment. 6. Both the isozyme I and II showed the different electrophoretic mobilities on immunoelectrophoresis. Rabbit anti-sera to isozyme II have been applied.