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골수의 Polyol 및 Sugar Dehydrogenase에 관한 연구
안병문,이희성,이근배,Ahn, Byoung-Moon,Lee, Hi-Sung,Lee, Keun-Bai 생화학분자생물학회 1979 한국생화학회지 Vol.12 No.1
토끼 골수의 homogenate를 분별원심 분리하여 세포질, mitochondria 및 핵분획을 분리하여 sorbitol dehydrogenase, adonitol dehydrogenase 및 mannitol dehydrogenase의 분포를 관찰하였으며 aldose 인 여러 당류에 대한 sugar dehydrogenase의 존재유무를 관찰하여 다음과 같은 결과를 얻었다. 1. Sorbitol을 D-fructose로, D-fructose를 sorbitol로 전환시키는 sorbitol dehydrogenase는 골수에 있어서는 D-fructose를 sorbitol로 촉매하는 작용만을 하며 mitochondria에만 존재한다. 2. Adonitol(ribitol) dehydrogenase의 활성도는 조직 1g 당 약 196 unit로 sorbitol dehydrogenase 및 mannitol dehydrogenase 보다 2.6배 및 41배 높았으며 세포질, mitochondria 및 핵분획에 각각 분포되어 있다. 3. Mannitol dehydrogenase는 조직 1g 당 4.78 unit로 활성도가 낮으며, 이 중 약 88%인 4.2 units가 세포질에 함유되어 있다. 4. Sugar dehydrogenae는 기질에 따라 특이성을 나타냈다. 즉, 조직 1g 당 효소활성도는 rhamnose>xylose>lactose>glucose>mannose>galactose>maltose의 순이며 rhamnose는 활성도가 20.14 unit/g으로 가장 높았고 trehalose에 대한 활성도는 전혀 없었다. Polyol dehydrogenases, i.e., sorbitol dehydrogenase, adonitol dehydrogenase and mannitol dehydrogenase of rabbit bone marrow were studied. Bone marrow was homogenized and the distribution of the enzyme activity in cytosolic, mitochonrial and nuclear fractions was measured. Sugar dehydrogenase activity in the crude preparations was also observed. The results obtained were as follows: 1. Sorbitol dehydrogenase activity which reduces D-fructose in the presence of NADH to D-sorbitol was localized in the mitochondria) fraction. The reverse reaction was inactive in both cytosolic and mitochondria) fractions. 2. Adonitol (ribitol) dehydrogenase activity (196 units/g wet tissue) was found to be approximately 3 times higher than that of sorbitol dehydrogenase and 40 times higher than mannitol dehydrogenase. 3. Mannitol dehydrogenase activity was very low (4.2 units/g wet tissue) and 88% of total activity was found in cytosolic fraction. 4. Sugar dehydrogenase were also examined in the crude preparation of bone marrow. he enzyme was most active with rhamnose (20.14 units/g wet tissue), but a number of other sugars was also good substrate. Dehydrogenation was effective in the following order of activity: rhamnose>xylose>lactose>glucose>mannose>galactose>maltose Trehalose did not serve as substrate.
골수의 Polyol 및 Sugar Dehydrogenase 에 관한 연구
안병문,이희성,이근배 ( Byoung Moon Ahn,Hi Sung Lee,Keun Bai Lee ) 생화학분자생물학회 1979 BMB Reports Vol.12 No.1
Polyol dehydrogenases, i.e., sorbitol dehydrogenase, ado:nitol dehydrogenase and mannitol dehydrogenase of rabbit bone marrow were studied. Bone marrow was homogenized and the distribution of the enzyme activity in cytosolic, mitochonrial and nuclear fractions was measured. Sugar dehydrogenase activity in the crude preparations was also observed. The results obtained were as follows: 1. Sorbitol dehydrogenase activity which reduces D-fructose in the presence of NADH to D-sorbitol was localized in the mitochondria) fraction. The reverse reaction was inactive in both cytosolic and mitochondria) fractions. 2. Adonitol (ribitol) dehydrogenase activity (196 units/g wet tissue) was found to be approximately 3 times higher than that of sorbitol dehydrogenase and 40 times higher than mannitol dehydrogenase. 3. Mannitol dehydrogenase activity was very low (4.2 units/g wet tissue) and 88% of total activity was found in cytosolic fraction. 4. Sugar dehydrogenase were also examined in the crude preparation of bone marrow. The enzyme was most active with rhamnose (20.14 units/g wet tissue), but a number of other sugars was also good substrate. Dehydrogenation was effective in the following order of activity: rhamnose $gt; xylose $gt; lactose $gt; glucose $gt; mannose $gt; galactose $gt; maltose Trehalose did not serve as substrate.
다중검출기 컴퓨터 단층 영상 분석을 이용한 Resident's ridge의 형태학적 연구
노정호,민병현,박정욱,안병문,Roh, Jeong-Ho,Min, Byoung-Hyun,Park, Jeong-Wook,Ahn, Byung-Moon 대한관절경학회 2008 대한관절경학회지 Vol.12 No.1
목적: 전방십자인대 재건술시 흔히 관찰하게 되는 Resident's ridge의 실제 형태학적 위치 및 모양을 알아보고자 한다. 대상 및 방법: 2007년 1월부터 2007년 8월까지 본원에서 시행한 48례의 정상 대퇴골 원위부를 촬영한 MD CT(Multidetector-Row Computed Tomography) 영상을 분석하였다. 과간절흔의 외측벽에서 1 mm 이상의 높이 변화를 보이는 경우를 Resident's ridge로 정의 하였다. $Lucion^{(R)}$ 프로그램을 이용하여 3차원 재구성한 영상을 통해 과간절흔의 전후방 길이, resident's ridge의 길이, 높이, 과간절흔의 후방 피질골로부터의 거리를 측정하였다. 결과: 환자의 평균 연령은 $59{\pm}16$세였으며 남성이 16례, 여성이 32례 이었다. Resident's ridge가 존재 하지 않았던 경우는 9례 이었으며 과간 절흔의 전후방 길이는 $25.4{\pm}3.5$ mm, Resident's ridge 의 길이와 높이의 평균값은 각각 $8.2{\pm}2.6,\;3.5{\pm}1.5$ mm 이었으며 Resident's ridge의 후방 피질골로부터의 거리는 $7.6{\pm}2.6$ mm 이었다. 결론: Resident's ridge는 많은 예에서 존재하며 뚜렷한 길이와 높이가 있기 때문에 전방십자인대 재건술시 주요한 landmark로 사용할 수 있다. Purpose: The purpose of this study was to report the real geometry of Resident's ridge doing in anterior cruciate ligament reconstruction Materials and Methods: From Jan 2007 to Aug 2007, 48 cases which had normal distal femoral condyle analyzed with Multidetector-Row Computed Tomography. Resident's ridge was defined as change of height above 1 mm in lateral wall of intercondylar notch. Anterior-posterior length of intercondylar notch, length and height of Resident's ridge, distance of Resident's ridge from posterior cortex were estimated with 3-D reconstruction using $Lucion^{(R)}$ program. Results: Cases were $59{\pm}16$ years olds and male was 16 cases, female was 32 cases. 9 cases had no Resident's ridge, anterior-posterior length of intercondylar notch was $25.4{\pm}3.5$ mm, average of length and height of the Resident's ridge was $8.2{\pm}2.6,\;3.5{\pm}1.5$ mm. Distance of the Resident's ridge from posterior cortex was $7.6{\pm}2.6$ mm. Conclusion: Resident's ridge was used as landmark in anterior cruciate ligament reconstruction, which presented in many cases and which had distinct length and height.
토끼골수의 Branched Chain Amino Acid Aminotransferase의 정제 및 성상
안병문,이동욱,이희성 중앙대학교 의과대학 의과학연구소 1982 中央醫大誌 Vol.7 No.2
The distribution and some properties of branched chain acid aminotransferase(EC 2.6.1.42)in rabbit bone marrow have been studied. Rabbit bone marrow was fractionated by differential centrifugation into nuclear, mitochondrial and cytosolic fractions. The activity of branched chain amino acid aminotransferase was measured by the method of Ichihara and Koyama. Isozyme pattern of this enzyme was also examined by DEAE-cellulose column chromatography. The results abtained were as follows; 1. The activity in homogenate was found to be 259.47 unit/g of wet tissue. The activity of this enzyme was relatively low compared with that in rat tissues, i.e., liver, heart, intestine and pancreas. 2. The distribution of branched chain amino acid aminotransferase in the subcellular organelles showed that 89.6% of the activity was in cytosolic fraction, 9.0% in mitochondral fraction and 1.4% in nuclear fraction. 3. Cytosolic fraction of rabbit bone marrow contained EnzymeⅢ, but not EnzymeⅠand Ⅱ, of branched chain amino acid aminotransferase, EnzymeⅢ was elluted by 200mM phosphate buffer from DEAEcellulose column and catalyzed the transamination of all three branched chain amino acids. 4. EnzymeⅢ was purified about 61-folds increase in specific activity after chromatography on DEAEcellulose. 5. The best substrate among the activity of the EnzymeⅢ was about 45℃ and the optomal pH was 8.2. 7. The Km values for leucine, isoleucine and valine of EnzymeⅢ were 1.37mM, 1.43 mM and 2.11 mM. respectively. 8. The Km values for α-ketoglutarate and pyridoxal phosphate of EnzymeⅢ were 1.03 mM and 2.17×10^-3 mM, respectively. 9. The molecular weight of EnzymeⅢ was estimated to be about 50,000 by polyacrylamide disc gel electrophoresis.