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Acetylcholine에 의한 적출 십이지장 평활근 수축에 미치는 Calcium 길항제의 영향
손의동,이만기,박창호,김인겸,김중영 慶北大學校 醫科大學 1991 慶北醫大誌 Vol.32 No.2
To compare antagonistic action of caloium antagonists on intestinal smooth muscle contraction, acetylcholine-induced phasic contraction (PC) and tonic contraction (TC) initiated by different calcium utilization were observed in the presence of various calcium antagonists by the use of isolated mouse duodenum suspended in Tyrode's solution. By verapamil at 2.2×10 exp(-6), 2.2×10 exp(-5) and 2.2×10 exp(-4) mM, PC was more decreased dose-dependently than TC. By nifedipine at 7.9×10 exp(-5) mM, PC was more decreased than TC, but at 7.9×10 exp(-6) mM it did not affect PC and TC. By diltiazem at 6.1×10 exp(-4) mM, PC was more decreased than TC, but at 2.4×10 exp(-4) and 2.4×10 exp(-5) mM it did not affect both of the contractions. By cobalt chloride at 0.3, 1.3, and 2.6 mM, TC was significantly decreased without affecting PC, but PC markedly decreased at 5.2 mM. These results reconfirmed the fact that cobalt ion-induced calcium antagonism is more related to calcium influx process than calcium release process in contrast with the actions of verapamil, diltiazem, and nifedipine in duodenal smooth muscle.
시금치 Glycolate Oxidase의 활성부위에 관한 연구
손의동,박양서,조태주,최정도,조남정,Son, Eui-Dong,Park, Yang-Seo,Cho, Tae-Ju,Choi, Jung-Do,Cho, Nam-Jeong 생화학분자생물학회 1994 한국생화학회지 Vol.27 No.5
Glycolate oxidase는 식물의 광호흡과정에 관여하는 효소 중 하나로서 glycolate를 glyoxylate로 산화시키는 반응을 매개한다. 시금치 glycolate oxidase에 대한 X-ray crystallography 연구에 의하면, histidine 254와 arginine 257이 효소작용에 중요한 역할을 수행하리라 추정된다. 이런 가설을 검증하기 위하여 본 연구에서는 site-directed mutagenesis 방법을 사용하여 이 효소의 histidine 254을 asparagine 또는 tyrosine으로, arginine 257을 serine으로 치환하였다. Wild type에서는 0.125mM의 기질에서도 강한 효소활성이 나타난 반면, mutant들의 경우에는 40mM 기질의 존재하에서도 효소활성이 거의 관측되지 않았다. 본 연구의 실험결과는 histidine 254와 arginine 257이 시금치 glycolate oxidase의 작용기작에 필수적인 아미노산이라는 것을 시사해 준다. Glycolate oxidase is one of the key enzymes in photo respiration, where it oxidizes glycolate to glyoxylate. Previous X-ray crystallographic studies on spinach glycolate oxidase suggested that histidine 254 and arginine 257 are important in the enzyme function. To evaluate this postulation, we replaced histidine 254 with asparagine or tyrosine and arginine 257 with serine by means of site-directed mutagenesis. The mutants xhibited little, if any, enzymatic activity with 40 mM glycolate, whereas the wild type showed a strong enzymatic activity in the presence of 0.125 mM glycolate. These results imply that histidine 254 and arginine 257 play essential roles in the action of spinach glycolate oxidase.
손의동,정지훈,김경태,조영래,민영실,송현주,제현동,임성혁,신용규,조성완 한국임상약학회 2006 한국임상약학회지 Vol.16 No.2
The aim of the present study was to evaluate the bioequivalence of two talniflumate preparations. We used Somalgen tablet (Kun Wha Pharmaceutical Co., Korea.) as a reference drug for bioequivalence of Crimain tablet (Samjini Pharmaceutical Ind. Co., Korea), and performed this whole study according to the guidelines of Korea Food and Drug Administration (KFDA). Twenty four healthy male volunteers, years in age and in body weight, were divided into two groups and a randomized cross-over study was employed. After one tablet containing 370 mg of talniflumate was orally administered, blood was taken at predetermined time intervals and the concentrations of talniflumate in plasma were determined using HPLC method with UV-detector. The analysis system was validated in specificity, accuracy, precision and linearity. These items of the analysis condition in this study conform to the guideline of KFDA. The pharmacokinetic parameters such as were calculated using the analysis condition we established and ANOVA test was utilized for the statistical analysis of the parameters using logarithmically transformed and Cmax. of reference drug and test drug in value were and respectively. The 90% confidence intervals using logarithmically transformed data were within the acceptance range of log(0.8) to log (1.25) for , respectively. These results indicate that Samjin talniflumate tablet is bioequivalent to reference drug, Somalgen tablet.
시금치 Glycolate Oxidase 의 활성부위에 관한 연구
손의동,박양서,조태주,최정도,조남정 ( Eui Dong Son,Yang Seo Park,Tae Ju Cho,Jung Do Choi,Nam Jeong Cho ) 생화학분자생물학회 1994 BMB Reports Vol.27 No.5
Glycolate oxidase is one of the key enzymes in photorespimtion, where it oxidizes glycolate to glyoxylate. Previous X-ray crystallographic studies on spinach glycolate oxidase suggested that histidine 254 and arginine 257 are important in the enzyme function. To evaluate this postulation, we replaced histidine 254 with aspamgine or tyrosine and arginine 257 with serine by means of site-directed mutagenesis. The mutants exhibited little, if any, enzymatic activity with 40 mM glycolate, whereas the wild type showed a strong enzymatic activity in the presence of 0.125 mM glycolate. These results imply that histidine 254 and arginine 257 play essential roles in the action of spinach glycolate oxidase.