PA-1 : STUDIES ON THE CHARACTERIZATION OF BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE FROM LENTINUS EDODES ( BERK . ) SING

배강규,민태진 한국생화학분자생물학회 (구 한국생화학회) 1987 추계학술대회집 Vol.- No.-

Poster Ⅰ : Purification and Characterization of Succinate - CoQ reductase ( Complex Ⅱ ) in Lentinus Edodes ( Berk . ) Sing

배강규,민태진 한국생화학분자생물학회 (구 한국생화학회) 1992 추계학술대회집 Vol.- No.-

The Structure and Antibiotic Activities of Hydroxy Acid of Lanostenol Compound in Daedalea dickinsii

배강규,민태진,Bae, Gang Gyu,Min, Tae Jin Korean Chemical Society 2000 Bulletin of the Korean Chemical Society Vol.21 No.12

31-Hydroxycarbowyacetylquercinic acid, a lanostenoid hydroxyl acid has been isolated from D. dickinsii by solbent extraction, silica gel column chromatography and recrystallization. The structure of this compound has been determined to be 31-hydroxycarboxyacetylquercinic acid by a combinationof spectral data and by HM-BC. This compound showed antimicrobial activities against human pathogenic fungi and bacteria.

띠미로버섯 중 25-Epi, $3{\alpha}-Carboxyacetylquercinic$ Acid의 분리정제, 구조결정 및 생리활성

배강규,민태진,Bae, Kang-Gyu,Min, Tae-Jin 대한화학회 2000 대한화학회지 Vol.44 No.1

띠미로버섯의 에탄올 추출물 중 25-Epi, $3{\alpha}-carboxyacetylquercinic$ acid의 두 구조, 항균활성 및 항암활성을 연구하였다. 화합물 1의 녹는점과 분자량은 각각 $167{\sim}168^{\circ}C$, 572였고, 몰 흡광 계수는 208 nm에서 5,040이었다. 여러 분광학적 성질로부터 이는 24S, 25S, $3{\alpha}-carboxyacetylquercinic$ acid로 확인되었고, 곰팡이, 효모 및 세균들에 대한 항균활성과 항암활성($IC_{50}=64.5\;{\mu}M$)이 있었다. 화합물 2의 녹는점, 분자량 및 몰흡광 계수는 각각 $233{\sim}235^<\circ}$, 572 및 208 nm에서 5,080이었다. 이는 24S, 25R, $3{\alpha}-carboxyacetylquercinic$ acid로 확인되었고, 화합물 1과 서로 다른 항균활성을 보였다. In order to develope bioactive substances, dried fmit body of Daedalea dickinsii collected from Taeback mountain was extracted with ethanol, The compounds 1 and 2 were purified by solvent extraction, silica gel column chromatography and recrystallization from the ethanol extracts. Melting point, molecular weight and molar extinction coefficient of the compound 1 were estimated to be $167{\sim}168^{\circ}C$, 572 and 5,040 at 208 nm. The structure of this compound 1 has been elucidated to be 24S, 25S, $3{\alpha}-carboxyacetylquercinic$ acid using spectroscopic properties. This compound showed antibiotic activities against fungi, yeasts and bacteria and it also showed anticancer activity $IC_{50}=64.5\;{\mu}M$) against Korean stomach cancer cell. Melting point, molecular weight and molar extinction coefficient of the compound 2 were estimated to be $233{\sim}235^<\circ}$, 572 and 5,080 at 208 nm. The structure of this compound was elucidated to be 24S, 25R, $3{\alpha}-carboxyacetylquercinic$ acid. The compound 2 showed different antibiotic activities with the compound 1.

버섯중 철이온에 활성화된 광감응성 Mitochondrial ATPase에 관한 연구

민태진,이미애,배강규 동국대학교 자연과학연구소 1993 자연과학연구 논문집 Vol.13 No.-

표고버섯중 광감응성 mitochondrial F?-ATPase는 Fe?, Fe? 및 M? 이온에 의하여 각각 활성화 되었으며 5.0mM Fe? 이온에 의한 상대활성도는 대조구에 비하여 107% 증가되었다. Mg? 존재하에서 Fe? 및 Fe? 각 이온 농도효과는 모두 효소의 활성을 증가 시켰으나 0.1mM Mg?과 5.0mM Fe? 이온의 공존하에서 170%를 증가시켜 Mg? 이온에 의한 상승작용을 보였다. 0.1mM Mg?과 0.1mM Fe? 존재하에서 Fe? 이온 농도효과는 그 농도가 5.0mM일 때 168%의 활성도 증가를 보여 Fe? 이온 공존 효과는 없었다. 이 효소는 Mg? 및 Fe? 이온에 으하여 활성화되는 특성을 가지고 있으며 활성 금속이온 존재하에서 측정한 최적 pH 및 온도는 각 각 7.5 및 66℃였다. The effects of the iron on the light-induced mitochondrial F?-ATPase in Lentinus edodes was studied. This enzyme activity was stimulated by each of the ferric, ferrous and magnesium ion. Especially, the activity of the enzyme by 5.0mF ferric ion increased up to 107% in comparision with control group(100%). In the presence of magnesium ion, each of ferric and ferrous ion increased the activity of the enzyme, particulary, coexistence of 0.1mM magnesium and 5.0mM ferric ion increased the activity up to 270% with magnesium ion dependence. The activity of the enzyme was stimulated up to 268% by 5.0mM ferric ionin the presence of 0.1mM magnesium and 0.1mM ferrous ion. Therefore, the coexistence of ferrous ion did not affect the activity. From the above, we propose that the light-induced mitochondrial F?-ATPase in L. edodes is a Mg?·Fe? f?-ATPase. The optimal pH and temperature for the enzyme were 7.5 and 66℃, respectively.

표고 버섯 중의 Branched chain amino acid Aminotransferase 의 분리정제 및 그 성질에 관한 연구

배강규,민태진,이수용 동국대학교 자연과학연구소 1987 자연과학연구 논문집 Vol.7 No.-

표고버섯중의 branched chain amino acid aminotransferase〔BCAT(EC 2,6,1,42)〕를(NH₄)₂SO₄ 분별침전, DEAE-cellulose column chromatography 및 sephades G-150겔 여과로 정제하여 그 특성을 조사하였다. 이 효소의 최적 pH는 8.5, 최적 온도는 36℃였고, 20℃이하에서 30분동안 열에 안정하였다. 이효소의 분자량은 69,000dalton이었으며, 산 가수분해하여 아미노산을 분석한 결과 18종의 서로 다른 아미노산들로 구성되어 있었다. 이 효소는 가지달린 아니노산인 L-valine, L-leucine 및 L-isoleucine에 대해서 특이성을 보였으며 phenylamine, potassium cyanide, phenylhydrazine, N-ethylmaleimide 및 p-chloromercuribenzoate에의하여 효소활성이 억제되었다. 또 한, L-leucine, a-ketoglutarate 및pyridoxal-5-phosphate에대한 이 효소의 Km값은 각 각 2.40mM, 2.98mM 및 1.74uM이었다. Branched cnain amino acid aminotransferaase 〔BCAT (EC 2.6.1.42)〕was purified by ammonium sulfate saturation. DEAE-cellulose column chromatography and sephadex G-150 gel filtration in Lentinus edodes(Berk.) Sing. Optimum pH and temperature were found to be 8.5 and 36℃, respectively. Apparent molecular weights of this enzyme was estimated 69.000 dalton by HPLC and SDS-PAGE. It showed activity toward L-leucine, L-isoleucine and L-valine as a substrate. It was ingibited by hydroxylamine, potassium cyanide, phenylgydrazine. N-ehylmaleimide, p-chloromercuribenzoate (CMB). cupric acetate and mercuric chloride. The Km values of this enzyme were determined to be 2.40mM for leucine, 2.98mM for a-ketoglutarate and 1.74μM for pyridexal-5- phospate, respectively.

β-Boswellic Acid 함유 제형의 자외선(UVB) 노출 피부 홍반진정 평가

배윤주,배강규,임은진 한국미용학회 2012 한국미용학회지 Vol.18 No.3

The purpose of this research is to observe healed effect of ingredient adding β-Boswellic Acid on erythema in human epidermis. Ingredient adding β-Boswellic Acid is obtained by diluting Boswellia Serrata resin in 1,3-Butylene Glycol. We examined erythema healing effect of Ingredient adding β-Boswellic Acid on human epidermis exposed to artificial UVB lights. Three Minimal Erythema Doses (MED) were induced on human epidermis by artificial UVB lights. In each area, we applied ingredient adding β-Boswellic acid (2.0 v/v%) and non-ingredient adding β-Boswellic Acid; one area remained to set reference value. The result of erythema healing effect of ingredient adding β-Boswellic Acid were obtained by comparing erythema progress after artificial UVB exposure on controlled epidermis. Our observation suggests that ingredient adding β-Boswellic Acid heals the erythema in human skin epidermis.

버섯 중 Aminotransferase 의 동질효소 분리정제 및 그 특성에 관한 연구 ( 1 ) - 표고버섯 ( Lentinus edodes ) 중의 Branched Chain Amino Acid Aminotransferase ( Enzyme 1 ) 의 정제 및 특성

민태진,배강규 ( Tae Jin Min,Kang Gyu Bae ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.6

Enzyme Ⅰ and Ⅱ of branched chain amino acid aminotransferase (BCAT) in Lentinus edodes (Berk.) Sing was purified by ammonium sulfate saturation, DEAF-cellulose column chromatography and sephadex G-150 gel filtration. We have been studied molecular weight, N-terminal amino acid, composition of amino acids, optimum pH, optimum temperature, K_m value and effect of organic compounds and metal ions about enzyme Ⅰ, to identify isozyme patterns between enzyme Ⅰ and Ⅱ. Apparent molecular weight of enzyme was estimated 69,000 dalton, N-terminal amino acid was determined glycine. The enzyme I was existed as negatively charged amino acids rather than positively charged ones by more than 7.13%. Optimum pH and temperature were found to be 8.5 and 30℃, respectively. It was stable for 30 min under 20℃. This enzyme showed activity toward L-leucine, L-isoleucine and L-Valine as a substrate. It was Inhibited by both organic compounds of hydroxylamine, N-ethylmaleimide and p-chloromercuribenzoate and metal ions of Cu^(2+), Hg^(2+) and Fe^(2+). The K_m values were determined to be 2.40 mM for L-leucine as a amino group donor, 0.30 mM for α-keto-glutarate as a amino group acceptor.

버섯 중 Aminotransferase 의 동질효소 분리정제 및 그 특성에 관한 연구 ( 2 ) - 표고버섯 ( Lentinus edodes ) 중의 Branched Chain Amino Acid Aminotransferase ( Enzyme 2 ) 의 정제 및 특성

민태진,배강규 ( Tae Jin Min,Kang Gyu Bae ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.6

Enzyme Ⅰ and Ⅱ of branched chain amino acid aminotransferase (BCAT) in Lentinus edodes (Berk.) Sing was purified by ammonium sulfate fractionation, DEAF-cellulose column chroma-tography and sephadex G-150 gel filtration. We have been studied molecular weight, N-terminal amino acid, composition of amino acids, optimum pH, optimum temperature, K_m value and effect of organic compounds and metal ions about enzyme Ⅱ, to identify isozyme patterns between enzyme Ⅰ and Ⅱ. Apparent molecular weight of enzyme Ⅱ was estimated 72,000 dalton, N-terminal amino acid was determined glycine. The enzyme Ⅱ was existed as negatively charged amino acids rather than positively charged ones by more than 3.67%. Optimum pH and temperature were found to be 8.2 and 38℃ , respectively. It was stable for 30 min under 20℃. This enzyme showed the activity toward L-leucine, as a substrate. It was inhibi-ted by both organic compounds of hydroxylamine, N-ethylmaleimide and p-chloromercuribenzoate and metal ions of Cu^(2+), He^(2+) and Fe^(2+). The K_m values were determined to be 3.39 mM for L-leucine as a amino group donor, 0.28 mM for α-ketoglutarate as a amino group acceptor. Although their molecular weight, N-terminal amino acid, composition of amino acids, optimum pH and temperature and K_m values had been different between enzyme Ⅰ and Ⅱ, but they showed same substrate specificity for L-leucine as a substrate.

버섯 중 Aminotransferase 의 동질효소 분리정제 및 그 특성에 관한 연구(II) -표고버섯(Lentinus edodes)중의 Branched Chain Amino Acid Aminotransferase(Enzyme II)의 정제 및 특성-

민태진,배강규,Min, Tae-Jin,Bae, Kang-Gyu 생화학분자생물학회 1992 한국생화학회지 Vol.25 No.6

Enzyme I and II of branched chain amino acid aminotransferase (BCAT) in Lentinus edodes (Berk.) Sing was purified by ammonium sulfate fractionation, DEAF-cellulose column chromatography and sephadex G-150 gel filtration. We have been studied molecular weight, N-terminal amino acid, composition of amino acids, optimum pH, optimum temperature, $K_m$ value and effect of organic compounds and metal ions about enzyme II, to identify isozyme patterns between enzyme I and II. Apparent molecular weight of enzyme II was estimated 72,000 dalton, N-terminal amino acid was determined glycine. The enzyme II was existed as negatively charged amino acids rather than positively charged ones by more than 3.67%. Optimum pH and temperature were found to be 8.2 and $38^{\circ}C$, respectively. It was stable for 30 min under $20^{\circ}C$. This enzyme showed the activity toward L-leucine, as a substrate. It was inhibited by both organic compounds of hydroxylamine, N-ethylmaleimide and p-chlromercuribenzoate and metal ions of $Cu^{2+}$, $Hg^{2+}$ and $Fe^{2+}$. The $K_m$ values were determined to be 3.39 mM for L-leucine as a amino group donor, 0.28 mM for $\alpha$-ketoglutarate as a amino group acceptor. Although their molecular weight, N-terminal amino acid, composition of amino acids, optimum pH and temperature and $K_m$ values had been different between enzyme I and II, but they showed same substrate specificity for L-leucine as a substrate. 표고버섯, Lentinus edodes (Berk.) Sing 중의 가지달린 아미노산 aminotransferase(BCAT)의 enzyme I과 II를 황산암모늄 분별침전, DEAE-cellulose column 크로마토그래피 및 Sephadex G-150 겔 여과하여 각각 분리정제한 후, enzyme I과 II의 동질효소 여부를 구명하기 위하여 enzyme II의 분자량, N-말단, 아미노산 조성, 최적 pH, 최적 온도, $K_m$값, 유기물 및 금속이온 효과 등을 실험하였다. 이 효소의 겉보기 분자량은 72,000 dalton 이었고, N-말단 아미노산은 L-leucine이었으며, 음성잔기를 가진 아미노산이 양성잔기를 가진 것보다 3.67% 더 많이 존재하였다. 최적 pH 및 최적 온도는 각각 8.2, $38^{\circ}C$ 였으며, $20^{\circ}C$이하에서 30분 동안 안정하였다. 이 효소는 기질인 가지달린 아미노산 중 L-leucine에 대해서만 활성을 보였으며, hydroxylamine, N-ethylmaleimide 및 p-chloromercuribenzoate 등의 유기물과 $Cu^{2+}$, $Hg^{2+}$ 및 $Fe^{3+}$ 등의 금속이온에 의하여 활성이 억제 되었다. 아미노기 공여체인 L-leucine과 아미노기 수용체인 $\alpha$-ketoglutarate에 대하여 활성도 측정시의 조건하에서 측정된 $K_m$값은 각각 3.39 및 0.28 mM이었다. 이로써 enzyme II와 I은 분자량, N-말단 아미노산, 아미노산 조성, 최적 pH 및 최적 온도 그리고 $K_m$값 등은 서로 다르지만, L-leucine 기질에 대하여 같은 기질 특이성을 보이는 효소였다.