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김형로 상상인 2022 상상인 Vol.- No.3

알코홀 대사에 미치는 Nicotinamide의 영향

金炯魯,池垠政,金禹現 전북대학교 의과학연구소 1980 全北醫大論文集 Vol.4 No.2

家兎 淋巴球 NAD Glycohydrolase의 硏究 : 1. 胸腺細胞 NAD Glycohydrolase의 性狀 1. Properties of NAD Glycohydrolase in Thymocytes

金炯魯,金禹現 전북대학교 의과학연구소 1979 全北醫大論文集 Vol.3 No.-

NAD glycohydrloase bound to the membranes of the rabbit thymocytes was solubilized and some properties of the solubilized enzyme were compared to those of the bound enzyme. More than 90% of bound NADase was solubilized by the treatment with 0.5% Triton X-100 to the intact thymochtes, while only 55% was solubilized by the action of pancreatic lipase. NADase solubilized by Triton X-100 has different properties from the bound NADase in optimal pH, and in inhibition by nicotinamide or isonicotinic acid hydrazide (INH). Optimal pH shifted from 6.8 in bound enzyme to 6.0 in solubilized enzyme. The concentration of nicoti-amide giving 505 inhibiton was increased from 6mM in bound NADase to 8mM in solubilized form. INH inhibited the activity of solubilized NADase more strongly than bound enzyme and, accordingly, brought the lesser formation of INH analogue of NAD in case of the solubilized NADase.

家兎赤血球의 Adenosine Diphosphate Ribose Pyrophosphohydrolase에 관한 연구

金炯魯,池垠政,金禹現 전북대학교 의과학연구소 1981 全北醫大論文集 Vol.5 No.2

Mg^2+ -dependent adenosine diphosphate ribose pyrophosphohydrolase(Mg^2+ -dependent ADPRase) from rabbit erythrocytes, which catalyzes the hydrolysis of adenosine diphosphate ribose(ADP-ribose) to AMP and ribose-5'-phosphate in the presence of divalent metal ions such as Mg^2+ or Mn^2+ was purified and its properties were characterized. 1. Mg^2+ -dependent ADPRase was partially purified 1331-fold to have the specific activity of 77.2μmoles per mg protein·Pr by ammonium sulfate fractionatior, DEAE-cellulose chromatography and Sephadex gel filtration. 2. The molecular weight of the enzyme was approximately 74,000 dalton determined by gel filtration on Sephadex G-100. 3. The enzyme showed a great substrate-specificity to ADP-ribose, while it did not hydrolyze the pyrophosphate bond of NAD, NADH, ADP, ATP and inorganic pyrophosphate, and phosphodiester bond of nitrophenyl-pT, indication that its true substrate in vivo is ADP-ribose. 4. The enzyme which has optimal pH of 9.5 was most stable at pH 6.2 in the pH range of the 5.4 to 8.6 with some loss of its activity during 2 hour incubation at 37˚.

家兎 肝의 Adenosine Diphosphate Ribose Pyrophosphohydrolase의 性狀

金炯魯,池垠政 전북대학교 의과학연구소 1979 全北醫大論文集 Vol.3 No.-

Adenosine diphosphate ribose pyrophosphohydrolase(ADPRase), which catalyzes the hydrolysis of ADPR to yield AMP and ribose-5'-phosphate was widely distributed in the cytoplasm of rabbit tissues. All the activity of ADPRase found in the cytoplasm of the erythrocytes was Mg^2+dependent and that of the kindey or the pancreas was Mg^2+independent, while cytoplasmic ADPRases of the liver consist of both the Mg^2+independent(92%) and Mg^2+independent(8%) form. Shown by the subcellular distributon of the Mg^2+independent ADPRase in the liver, 65% of the total activity was found in the nucleus, 20% in mitochondria, and 15% in cytoplasm. Cytoplasmic or nucleal Mg^2+independent ADPRase of the kidney was specifically inhibited by AMP but not by ATP at all, while both forms of ADPRase of the liver were inhibited not only by AMP but by ATP to the larger extent. It is proposed that Mg^2+independent ADPRase would convert to Mg^2+independent form by the storage of this enzyme at 4℃, showing that the activity of the dependent form became the same as independent form if stored a day and further increasement of independent form attained to the 85% of the total activity in five days storage.

J. Conrad의 The Nigger of the 'Narcissus'에 관한 소고 : 인물을 중심으로

김형로 원광대학교 교육대학원 1990 硏究論叢 Vol.1 No.-

Vibrio vulnificus가 분비하는 Cytolysin에 관한 연구

김형로,김우현,노혜원,김강신,박인숙 의과학연구소 1988 全北醫大論文集 Vol.12 No.1

The extracellular cytolysin produced by Vibrio vulnificus isolated from a patient with primary sepsis was partially purified and its properties were studied. 1. The cytolysin production in culture supernatant reached to the maximum of 800HU/ml at 5 hours' culture and was reduced by the addition of NaCl in culture media. 2. The cytolysin was heat-labile and completely inactivated when stored at 4℃ for 24 hours but the stability was greatly enhanced by the addition of glycerol(50%) or bovine serum albumin(mg/ml). 3. The cytolysin in culture supernatant was partially purified 40 folds to the specific activity of 32570HU/mg protein by ammonium sulfate precipitation, calcium-phosphate gel adsorption and DEAE-cellulose chromatography. 4. The cytolysin was lethal for mouse(18HU/mouse), but pretreatment with verapamil or Tavegyl 1 hour before the injection of cytolysin significantly prevented the lethal effect of cytolysin.

적혈구의 막 단백에 관한 연구 1. 가토 적혈구 NAD Nucleosidase의 정제와 요소에 의한 부활현상

김형로,Kim, Hyung-Rho 생화학분자생물학회 1973 한국생화학회지 Vol.6 No.1

가토적혈구막 NAD nucleosidase (NADase)를 췌장 lipase로 가용화시켜 부분 정제하여 이 효소의 일부성상을 구영하였다. 췌장 lipase를 무손상가토적혈구에 작용시키면 적혈구의 파괴없이 막 NADase가 쉽게 가용화되어 효소활성이 소실되지 않고 유리되었다. 이는 NADase 분자전체가 적혈구막외연에 위치하고 있음을 시사해 주고 있다. 적혈구막 NADase를 lipase로 가용화시 킨 다음 26배 부분정제하여 그 성상을 관찰한 바, 이 효소는 저농도의 urea에 의하여 효소활성이 현저히 부활되었으나 가토의 다른 조직 NADase나 다른 포유동물의 적혈구막 NADase는 urea에 의하여 전혀 활성화되지 않았다. 0.2M urea는 NADase의 NAD에 대한 Michaelis 정수 (Km 치)와 최고반응속도 (Vmax)를 3배가량 동일한 율로 증가시켜 1/s에 대한 1/v의 double reciprocal plot에 있어서 urea 유무시의 양 직선이 서로 평행하였다. NADase의 상경성 저해제인 NADP와 nicotinamide mononucleotide (NMN)는 urea의 부활작용을 전혀 소멸시키지 못하였으나 비상경성 저해제인 nicotinamicle와 3-acetylpyridine은 urea의 부활작용을 거의 소멸시켰다. 이와같은 실험성적은 urea가 NADase의 uncompetitive activator로 작용하여 효소-기질복합체 형성반응에는 무관하고 효소-기질복합체의 분해 과정중에서 nicotinamide가 유리되는 단계를 촉전시키는 것이라고 시사되었다. When intact rabbit erythrocytes were treated with pancreatic lipase, the membrane-bound NAD nucleosidase (NADase) was partially solubilized without marked destruction of the cellular stucture, suggesting that the entire molecule of the rabbit erythrocyte NADase is located on the outer portion of the cell membrane. The lipase-solubilized NADase from rabbit erythrocyte membrance was partially purified 26-fold, and its properties were characterized. Among other properties the most characteristic one was that the rabbit erythrocyte NADase was activated by urea in low concentrations, whereas NADases from other sources were not affected. Urea (0.2 M) caused three-fold increases in both the Michaelis constant for NAD and the maximal velocity of NADase, thus making the reciprocal plot in the presence of urea parallel to the plot in the absence of urea. The competitive inhibitors such as NADP and nicotinamide mononucleotide did not eliminate the activation effect of urea, while nicotinamide and 3-acetylpyridine known as noncompetitive inhibitor eliminated the urea effect. These results strongly imply that the activation of NADase by urea in low concentrations is of uncompetitive nature, suggesting that the action of urea should enhance the rate of the enzyme-substrate complex breakdown involved in the liberation of nicotinamide and not earlier step concerned with the formation of the enzyme-substrate complex.

大學에 있어서의 誠信義敎育과 人間改造

김형로 건국대학교 농과대학 연합학회 1968 건농 Vol.- No.2

인간은 탄생과 동시에 그 본래의 선천성을 지니며 개체본연의 고질성을 얻게된다. 낙지이후부터 존재하는 동안의 개체는 환경의 영향을 받아 선천성과 유기적으로 중용화하는 후천성을 겸유하게 된다. 무릇 인간의 성장과정에는 이러한 내적 외적이며 선천후천의 갈등속에서 시시각각으로 하나의 인간유형으로 조성되어 가는 것이다. 여기에 윤리와 도덕의 본선에 입각한 정궤도의 사회인으로서의 인간형성의 배양과 인격도치의 안내자로서 교육이 등장하게 된다. 교육은 생장의요 발전임으로 인간개체에 대한 침투주입적향상의 역학을 하면서 거칠고 세련되지 못한 야생적 인간을 품격높고 세련된 2차원의 세계에도 진입시키는 것이다. 그러므로 인간은 인격도치의 마당에서 필연코 선행해야 되는 교시가 정립되지 않으면 안된다. 언제 어디서든지 인간의 세계에는 좌우명적인 교시가 존재해야하는 것이다. 초등과 중등교육을 화함으로써 사회의 일원으로서 구성원은 되나 고등교육인 대학교육에 있어서는 일국의 국가사회를 우한 지도적인물을 양성하는 곳이므로 필요불가결한 의념의 존재하지 않으면 안된다. 인간교육의 최종적인 「건국」교시인. 성•신•의는 인간의 궁극적인 목적 필연사인 것이 될 것이다.

Ornithine Aminotransferase의 活性 測定法 考案

金炯魯,李桂貞,朴鎭宇 전북대학교 의과학연구소 1981 全北醫大論文集 Vol.5 No.1

An attempt was made to develop a new assay method for ornithine aminotransferase which catalyzes the transfer of δ-amino group in ornithine to α-ketoglutarate to yield glutamate-γ-semialdehyde and glutamate. Glutamate-γ-semialdehyde (or pyrroline-5'-carboxylic acid), one of the reaction products was found to produce a colored compound showing a peak absorbance at 510nm with ninhydrin in hot acidic solution, whereas ornithine of glutamate didn't produce any colored production indicated that the enzyme activity could be properly assayed by reading the change of absorbance at 510nm. The enzyme activity measured by the new assay method was widely distributed in mouse tissues, especially high in cytoplasmic fraction of small intestine and kidney, and in mitochondrial fraction of liver. The enzyme activity showed increasing tendency in liver and kidney with age in contrast to decreasing tendency in small intestine.