지방의 에너지대사

곽상태 대한운동학회 2002 아시아 운동학 학술지 Vol.- No.12

위계문화가 임파워먼트 및 조직유효성에 미치는 영향에 관한 실증연구 - 건설산업 중심으로 -

곽상태,양동우 한국디지털정책학회 2016 디지털융복합연구 Vol.14 No.3

사람 태반조직 DNA Topoisomerase Ⅰ에 대한 Phosphorylation의 영향

곽상태,김승민,박종일,손미영,임규,황병두 충남대학교 의과대학 지역사회의학연구소 1996 충남의대잡지 Vol.23 No.2

DNA topoisomerase I was prepared from human term placenta and the effects of phosphorylation/dephosphorylation to the enzyme activity have been investigated. hosphorylation of the enzyme by protein kinase'A or casein kinase II did not affect the activity of DNA topoisomerase I. But dephosphorylation of the enzyme by calf intestinal alkaline phosphatase decreased the DNA topoisomerase I activity. The inhibitory effects of camptothecin or 10-OH-camptothecin on the enzyme were not related to dephosphorylation of the enzyme. These results suggest that DNA topoisomerase I from human term placenta present in forms of phosphorylated, and regulation of the enzyme activity is related with phosphorylation/dephosphorylation of the enzyme.

온라인 피부과학 이미지 데이터베이스의 개발

곽상태,이웅재,정회경,조인준,이증훈,박장규,서기범 대한피부과학회 1999 大韓皮膚科學會誌 Vol.37 No.12

Background:Most dermatologic diseases are diagnosed based on typical clinical and histopathologic features. Consequently, image databases for these diseases are necessary for educational and diagnostic purposes. Objective:To establish a general visual reference for dermatologic diseases and supporting materials for basic medical education. Methods:Approximately 2000 clinical images were selected from our archive of 50,000 slides. These images were digitized and catagorized according to the key system developed by the Department of Dermatology, Erlangen University with minor modification. The architecture and components of this image database are presented in this paper. Results:The database allows a search for appropriate dermatologic images according to diagnosis, localisation, and appearance of skin lesions. Conclusion:We have established a WWW (world-wide-web) based online dermatologic image database which can be used as a useful tool for general reference and for educational material.

胎盤組織 Cytidine Deaminase에 關한 硏究

郭相太,黃炳斗 충남대학교 의과대학 지역사회의학연구소 1986 충남의대잡지 Vol.13 No.1

Cytidine deaminase(EC 3.5.4.5) was isolated two isoenzymes having molecular weight 1,000,000(CDase Ⅰ) & 90,000 (CDase Ⅱ), and patially purified 28 & 11 folds respectively by combination of amonium sulfate precipitation, sephacryl S-300 chromatography and adsorption to calcium phosphate gel, and then their properties are investigated. 1. pH optimum of CDase Ⅰ is around 7.2, but CDase Ⅱ exhibit broad from 5 to 9. 2. CDase Ⅱ, heat stable, remains 80% of activity against heat treatment at 80℃ for 5 minutes, but CDase Ⅰ is relatively heat labile. 3. The activity of CDase Ⅱ is decreased to 27% by addition of 3 units of proteinase in the reaction mixture, whereas CDase Ⅰ remains 69% of its activity. 4. The activity of both enzymes are inhibited by Cu^2+, increased by Ca^2+ and little affected by other cations. 5. Both enzymes are inactivated in prerence of 2mM p-hydoxymercuribenzoic acid, but previously 4mM mercaptoethanol added enzyme solution is not inactivated. 6. Polyamines markedly promote the activity of CDase Ⅰ, but, except spermidine, inhibit the activity of CDase Ⅱ. 7. The apparent Michaelis constant of both enzymes is identical for cytidine 5.5×10^(-5) M and for deoxycytidine 3.5×10^(-5) M. From the above results, CDase from human placenta is identified two isoenzymes and its properties are compared with those of the other tissue CDase.

水晶體 β-Crystallin의 Aggregation에 對한 Calcium의 影響에 關한 硏究

元相喜,郭相太,林圭 충남대학교 의과대학 지역사회의학연구소 1988 충남의대잡지 Vol.15 No.2

Changes of protein patterns of CaCl_2-treated β-crystallin fraction and native β-crystallin frac tion, and the effects of mercaptoethanol have been investigated by urea/polyacrylamide gel electrophoresis (urea/PAGE). 1. Physiological concentration (0.8 mM) CaCl_2- treated β_H-crystallin was separated seven subfra ctions by urea/PAGE. In the 10 mM CaCl_2- treated β_H-crystallin, No. 6, 7 subtractions were dec reased and No. 6B subfraction was newly appeared when compared with that of 0.8 mM CaCl_2- treated. In the presence of 20 mM EGTA, protein patterns exhibited the same as 0.8 mM CaCI_2- treated native β_H-crystallin. In 10 mM CaCl_2-treated β_H-crystallin, No. 7 subfraction was decrea sed and No. 6B subfraction was appeared. 2. Physiological CaCI_2 concentration (0.8 mM)-treated β_L-crystallin was separated nine subfrac tions by urea/PAGE. In the high CaCI_2 concentration (10 mM)-treated β_L-crystallin, No.9 subfraction was disappeared and No. 8 subfraction decreased. In the presence of 20 mM EGTA, proteinpatterns exhibited the same as 0.8 mM CaCl_2- treated β_L crystallin. In 10 mM CaCl_2- treated native β_L-crystallin, No. 8B subfraction was disappeared and No. 8A subfraction was increased. 3. When β-crystallin separated after 10 mM mercaptoethanol and 10 mM CaCl_2- treated was electrophoresed by urea/PAGE, No. 6, 8 subfractions were disappeared and No. 3, 7 subfraction were increased in β_H-crystallin, and No. 5 subfraction was increased in β_L-crystallin From the above, results it is suggested that the aggregation of β-crystall ins of the lens by calcium may be resulted to not only the interaction of α, γ-crystallin subfra ctions, but also the interaction of β-crystallin subfractions, and not related the formation of disulfide bond.

STUDIES ON S - ADENOSYL - L - METHIONINE : PROTEIN - CARBOXYL O - METHYLTRANSFERASE FROM BOVINE RENAL CORTEX

송만수,곽상태,임규,이재흔,황병두 한국생화학분자생물학회 (구 한국생화학회) 1987 추계학술대회집 Vol.- No.-

心臟組織 Protein Methylase Ⅱ의 精製 및 性狀

임규,곽상태,황병두 충남대학교 의과대학 지역사회의학연구소 1985 충남의대잡지 Vol.12 No.2

Protein methylase II han been purified from bovine heart approximately 13,100 folds with a 17% yield by combination of ammonium sulfate precipitate, sephadex G-75 chromatography, S-adenosylhomocysteine-sepharose 4B chromatography, hydroxyapatite chromatography. The enzyme shows a rH optimum around 6.2. The enzyme is heat labile, inactivated by heat treatment for 5 minutes at 70℃, and when stored at -20℃ in the presence of 10% glycerol, approximately 40% of activity has been lost in a year. Copper ion(Cu^2+) is a rotent inhibitor, the activity being inhibited 85% at 2 mM and 25% of the inhibition is recovered by addition of 4mM EDTA, and ferrous ion(Fe^2+) also inhibits 40% at 2 mM. The other metal ions almost do not inhibit. The lam value for S-adenosy l-L-methionine is 5 × 10 exp(6)M. Histone II A-S and calmodulin are good substrates for this enzyme. Calmodulin of bovine heart is methylated by this enzyme and 5.5 pmoles of 〔^14C〕methyl group is incorporated per 50㎍ calmmdulin after 30 minutes incubation.

骨格筋 Protein Methylase Ⅱ에 關한 硏究

洪承元,郭相太,林圭,黃炳斗 충남대학교 의과대학 지역사회의학연구소 1988 충남의대잡지 Vol.15 No.2

Protein methylase Ⅱ (S-adenosy-L-methionine : protein-carboxyl 0-methyltransferase) has been, purifed 6,600-fold from bovine skeletal muscle and characterized. The purification procedures involved ammonium sulfate fractionation, Sephadex G-75 chromatography, S-adenosyl-L-homocysteine-Sepharose 4B chromatography, and hydroxyapatite chromatography. The enzyme showed an optimal pH around 6.0. It was heat-labile, being inactivated by heattreatment at 60℃ for 6 minutes. However, storage of the enzyme at -20℃ in the presence of 10% glycerol prevented the activity loss for 6 months. The apparent Km for S-adenosyl-L-methionine was 2.86 × 10 exp (6) M. Copper(Cu^2+) ion was potent noncompetitive inhibitor, the activity being completely inhibited b) 0.25 mM Cu^2+ and 1 mM Zn^2+. Most of the activity loss by copper and zinc ions were recovered by the addition of ethylenediamine tetracetate. The enzyme was also completely inhibited by 0.5 mM phydroxymercuribenzoate, which could be reversed by the addition of 10 mM 2-mercaptoethanol. The molecular weight of the enzyme was 24,000, as determined by Sephadex G-75 chromatography. Histone IIA, immunoglobulin A and soybean trypsin inhibitor were efficiently carboxylmethylated by the enzyme. Sarcoplasmic reticulum(SR) and sarcolemma(SL) of the skeletal muscle were also efficiently carboxylmethylated by the enzyme at a rate of 0.96 and 0.63 pmolesl mg protein/min of 3^H-CH_3, incorporation, respectively. Polyacrylamide gel electrophoresis of the carboxylmethylated SR and SL revealed multiple carboxylmethylated subfactions : SR resolved into the subfractions with molecular weight 100,000, 55,000, 22,000 and 14, 400, and SL into the subfractions with molecular weight 48,000, 22,000 and- 14, 400. Of these subfractions those with Mr=22, 000 were most strongly carboxylmethylated. Endogenous cAMP-dependent phoshorylation of SR occurred in the subfractions with Mr=55, 000, Mr=27, 000 and Mr=~14, 400, of which the fraction with Mr=27, 000 was most strongly phosphorylated. When SR was carboxylmethylated, the endogenous cAMP-dependent phosphorylation was decreased. SR exhibited relatively high Ca^2+-ATPase activity and oxalate-facilitated ATP-dependent 45^Ca^z+uptake. The carboxylmethylation and cAMP-dependent phosphorylation of SR increased the Ca^2+TATPase activity by 15% and by 29%, respectively. However, cAMP-dependent phosphorylation of SR which had been previously carboxylmethylated led to only 23% increase in the Ca^2+-ATPase activity. Both the carboxylmethylation and cAMP-dependent phosphorylation enhanced the steady-state rate as well as the initial rate of ^45Ca^2+-uptake. Kinetic analysis showed that the apparent Km and Vmax of Ca^2+ for ATP-dependent Ca^2+-uptake were 45μM and 35 nmoles/mg protein, respectively. Both the carboxylmethylation and cAMP-dependent phosphorylation of SR decreased the Km and increased the Vmax for the Ca^2+-uptake. These results suggest that protein methylase II might have some regulatory role in the calcium transport of sarcoplasmic reticulum.

胎盤組織 Cytidine Deaminase에 關한 硏究 (Ⅰ) : Purification & Characterization

황병두,곽상태,임규,이재흔,백문기 충남대학교 의과대학 지역사회의학연구소 1984 충남의대잡지 Vol.11 No.2

Cytidine deaminase has been partially purified from human term placenta approximately 26-fold by combination of ammoninm sulfate saturation, sephacryl S-300, DEAE-cellulose and hydroxyapatite chromatography, and then its properties have been investigated. The enzyme shows a broad optimum pH from 5 to 9 and is heat-stable being, almost remained its activity by heat treatment at 70℃ for 8 minutes. The enzyme activity is inhibited to 23% and 77% by 2 mM of Cu^2+ and Co^2+, respectively, but, other cations do not affect the enzyme activity. The apparant Michaelis constant for cytidine and deoxycytidine are 74 uM and 69 uM, respectively. Kinetic analysis of cytidine deminase in presence of 0.25 mM Cu^2+ shows that the nature of the inhibition to cytidine deaminase is competitive, considering that Vmax is independent while km value is increased. The enzyme activity is completely inhibited by 0. 5 mM of p-hydroxymecuribenzoicacid(PHMB)but all of the activity is recovered in adding mercaptoethanol. The enzyme activity is decreased about 50% in prescence of 5 mM of polyamines. The enzyme activity is mainly located in the nuclei (80%) and cytosol(16%) fractions. he molecular weight of the enzyme is about 770, 000.