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李天培,朴文奎,金演斗,金天漢 충남대학교 자연과학연구소 1978 學術硏究誌 Vol.5 No.2
A simple and accurate method is presented for the determination of trace levels of rhenium metal in copper sulfide ores. Roasting of the samples with calcium oxide at 700 C shows an effective method of decomposition for the subsequent determination of Re-dimethylglyoxime complex by spectrophotometry.
DEAE-Cellulose에 의한 Serum Trypsin Inhibitor와γ^(e)-Globulin의 分離
李天培 충남대학교 자연과학연구소 1975 學術硏究誌 Vol.2 No.2
To study the antitrypsin and antisoybean trypsin inhibitor, we have improved the estimation method of trypsin and soybean trypsin inhibitor. Trypsin activity was determined in good stability and reproducibility by using the 0.05M Phosphate buffer (pH8.0)and 1% Casein solution as substrate without Ca^(++) ion. The quantity of soybean trypsin inbitor was found by measuring the degree of inhibition of trypsin activity. Serum trypsin inhibitor and non specific protease in serum were removed by treating with DEAE-cellulose which had been bufferized with 0.0175M phosphate buffer (pH 6.3) but r^(e)-globulins of anti AαA or anti TAA were remained 90% or above.
Geraninm sibiricum L.의 抗眞菌作用에 관한 硏究
李天培,朴文奎,白承和 충남대학교 자연과학연구소 1976 學術硏究誌 Vol.3 No.2
The water and methanol extracts from Geranium sibiricum L. which is widely spread plant in Korea were examined for the inhibitory activities against pathogenic dermatopathy. The fungicide activities were shown to be strong and were not decreased with treatment at 120℃ and 2 atm. The chemical components of the plant known so far did not show the activities, and the isolation of the other effective ingredients is under study.
p-Nitrostyrylphenylsulfone 基質에 對한 L-Cysteine의 反應
李天培,成洛道,明平根 충남대학교 자연과학연구소 1980 學術硏究誌 Vol.7 No.1
The kinetics and mechanism of nucleophilic addition of L-Cysteine to P-nitrostyrlphenyl-sulfone substrate over wide pH range was presented and analyzed in detail. The rate constants were determined by ultra-violet spectrophotometry in 50% methanol water mixed solvent at 25℃ and the following rate equation which can be applied over wide pH range was obtained. i.e kt = ko + kp [OH^(-)] =(1.92×10^(-3)+3.71×10^(3)[OH^(-)]/8.94×10^(-2)+1.03×10^(5)[OH^(-)]) +4.56×10^(2)OH^(-)] From the rate equation, the following mechanism were proposed; above pH 10. 50, the reaction proceed by the attack of L-Cy-S^(-) on the activated carbon-carbon double bind of substrate. Below pH 8.50, the reaction proceed by addition of L-Cysteine to p-nitrostyrl phenylsulfone substrate. And in the range of pH 8.50-10.50, these two reaction occur competitively.
李天培,權奇星,朴文奎 忠南大學校 1974 論文集 Vol.13 No.1
Instant ginseng tea and two sorts of ginseng extract powders which were sold in drug stores as tonics were administered to rats and compared with control group which were administered saline only. Blood sugar contents of instant tea administered group were lowered about 10% after 6 to 8 hours from dose than control group, but those of ginseng extract powder administered group were lowered about 30% after 4 to 6 hours. Glycogen contents of liver also exhibited as blood sugar and ginseng extract powder administered groups were lowered about 60% than control group. But blood sugar and glycogen contents were recovered to the normal value after 12 to 24 hours.
Thiocholine ester 기질을 이용한 Acetylcholinesterase 활성부위의 구조특성
이천배,주은희,최수라,석대은,명평근 충남대학교 기초과학연구소 1999 忠南科學硏究誌 Vol.26 No.1
The inhibition pattern of three inhibitors(tacrine, decamethonium and propidium) on the hydrolysis of various thiocholine ester substrates by eel acetylcholinesterase was comparatively examined. When the substrate was acetylthiocholine, it showed a similar competitive inhibition by tacrine inhibitor, and a mixed type inhibition by decamethonium and propidium inhibitors. When the substrate was pentanoylthiocholine, it showed an uncompetitive inhibition by tacrine, and a noncompetitive inhibition by decamethonium. When the substrate was laurylthiocholine, it showed mixed type and uncompetitive inhibition by tacrine, and a competitive inhibition by decamethonium and propidium. Those results suggest that the active site of acetylcholinesterase has the existence of hydrophobic site besides the anionic and esteratic site.