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RISS 인기검색어
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- 저자 : T. J. Min(閔泰鎭) (검색결과 4 건)
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H. B. Kim(金興培),K. J. Kim(金炅濟),T. J. Min(閔泰鎭) 한국육종학회 1973 한국육종학회지 Vol.5 No.1
Different levels of Ethrel and RH-531 were applied on the leaves of winter barley at booting stage. Both peduncle length and plant height were significantly reduced at high levels of the chemicals. Plant height was highly correlated with (r=1) peduncle length. Grain weight also was influenced by the chemicals and more grain weight was obtained from treated plant than check. Crude protein percentage in the kernel was decreased by RH-531 but no effect by Ethrel.
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야생연어(Salmo Salar) 알 중의 Carboxypeptidase A 의 특성에 관한 연구
김준행,민태진 동국대학교 자연과학연구소 1985 자연과학연구 논문집 Vol.5 No.-
야생 연어알중의 carboxypeptidase A를 CM-cellulose, (NH₄)SO₄ 0.5포화, DEAE-cellulose column 크로마토그라피 및 Sephadex G-75 겔 여과에 의하여 분리 정제하여, 그 특성을 조사하였다. 야생 연어알로부터 2종류의 활성분획 A 및 B를 얻었다. 활성분획 A는 bovine hemoglobin 및 hippuryl-L-phenylalanine과 같은 기질에 대하여 활성을 보였다. 이 효소의 분자량은 44,000 dalton이었으며, 18종의 아미노산으로 구성되여 있는 단량체였다. 최적 pH는 4.5, 최적 온도는 60℃였고, pH2.5~3.5, 20~60℃에서 안정하였다. 이 효소는 glycyl-L-phenylalanine의 펩티드 결합을 분해시키는 특이성을 보였으며, Km값은 0.29mM이였다. Fe³및 L-cysteine에 의하여 저해받았으며, L-cysteine은 경쟁적 저해제였고, 그의 Ki값은 1.2mM이였다. The enzymic properties of Carboxypeptidase A in the Eggs of Salmon (Salmo Salar) were investigated by purification with CM-cellulose, ammonium sulfate fractionation (50%), DEAE-cellulose and Sephadex G-75 gel filtration. Two kind of active fraction A and B were isolated from the egg of wild salmon. The fraction A showed its activity toward substrate such as bovine hemoglobin and hippuryl-L-phenylalanine. The molecular weight of this enzyme was determined to be 44,000 daltons by SDS-PAG electrophoresis and the enzyme was monomeric protein composed of 18 amino acids. Optimum pH was 4.5, optimum temperature was 60℃, and the enzyme was stable at PH 2.5~3.5 and 20℃-60℃ This enzyme showed substrate specificity hydrolyzing the peptide bond of glycyl-L-phenylalanine. Its Km value was 0.29 mM and the enzyme was ingibited by Zn, Fe and L-cysteine. The L-cysteine was found to be competitive inhabitor, and its Ki value was determined to be 1,2 mM by Dixon plot.
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리신, 페닐알아닌등에 의한 茯笭(poria cocos (schw.) Wolf)중 Carboxyl proteinase의 저해효과
박상신,민태진 동국대학교 자연과학연구소 1985 자연과학연구 논문집 Vol.5 No.-
복령(Poria cocos(cshw.) wolf) 중의 carboxyl proteinase를 NHSO 0.65포화, DEAE-cellulose 및 Sephadex G-75 겔 여과르 정제하여 그 특성을 조사하였다. 이 효소는 Carbobenzoxy-L-glutamyl-L-tyrosine의 glutamyl-L-tyrosine 사이의 펩티드 결합을 가수분해 하는 특이성을 보였으며, Zn??, Ca??, Mg??, CN??, P?O??등의 이온은 효소의 활성을 저해하였으나, Hg??은 효소의 활성을 증가시켰다. L-lysine, L-phenylalanine, hippuryl-L-phenylalanine, diazoacetyl-DL-norleucine methylester 및 1,2-epoxy-3-(P-nitrophenoxy) propane등의 유기화합물들은 효소의 활성을 크게 저해하였다. L-lysine, L-phenylalanine 및 hippuryl-L-phenylalanine ,등은 항온처리시간의 증가에 따라 효소의 활성을 점차 감소시켰고, 특히 L-Lysine은 20분 까지 급격히 저해하였으며, Cu?? 공존하에서의 DAN은 Cu?? 이 없을 때의 DAN에 비하여 30분 이후부터 활성을 감소시켰다. L-lysine은 이 효소에 대하여 경쟁적 저해작용을 하였으며, Ki 값은 0.12m mole 이었다. The properties of carboxyl proteinase which is contained in poria cocos (Schw.) Wolf were investigated by means of the purification with 0.65 ammonium sulfate saturation, DEAE-cellulose and Sephadex G-75gel filtration. This enzyme was found to hydrolyze only peptice bond between glutamyl-L-tyrosine of cabobenzoxy-L-glutamyl-L-tyrosine among the synthetic substrates of carbobenzoxy-L-glutamyl-L-tyrosine, hippuryl-L-phenylalanine and hippuryl-L-arginine. This enzyme was inhibited by Zn??, Fe??, Ca??, CN??, P?O?? ion etc, but stimulated by Hg?? ion. Also, this enzyme was inhibited by organic compounds such as L-lysine, L-phenylalanine, hippuryl-L-phenylalanine, diazoacetyl-DL-norleucine methyl ester (DAN) and 1,2-epoxy-3-(-nitrophenoxy) propane (EPNP). In Particular, the activity was inhibited by L-lysine till 20 minutes of preincubation time rapidly, and by DAN in the presence of Cu?? ion more rapidly after 30 minutes than DAN in the absence of Cu?? ion. The L-lysine was found to be a competitive inhibitor and its Ki value was determined to be 0.12 mmole by Dixon plot.
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조석우,민태진,이갑득 동국대학교 자연과학연구소 1987 자연과학연구 논문집 Vol.7 No.-
표고버선의 미토큰드리아는 설탕밀도 선형기울기 원심분리법으로 정제하여, 광감음성 mitochondrial ATPase의 유기물 효과, 광증감제 효과 및 파장변화에 따른 K 이온의 유입효과를 실험하였다. 1.이 효소는 10mmol dithiothreitol, 및0.1mmol quinacrine에 의하여 각각 139% 및 128%의 활성도를 증가시켰다. 2.100ug의 oligomycin과 1mmol phlorizin은 이효소의 활성을 각각 48% 및 45%억제 시켰다. 3.광증감제인 0.1mmol phenazine methosulfate는 이 효소의 활성도를 36% 촉진시켰다. 4.K이온 유입 효과의 최적 파장은 690nm였고, 이때의 최적 pH 및 최적 온도는 각각 7.2 및 55%였다. Effects of organic compound, photosentizer and K in influx on the light-induced ATPase of mitochondria in L. deodes purified by linear sucrose density gradient centrifugation were studied. The motochondrial ATPase activity was investigated by various wavelength illumination at dark state. The mitochlndrial ATPase was activated 139% and 128% by 10mmol dithiotheitol and 0.1mmol quinacrine, respectively. This enzyme also was activated 36% by 0.1mmol phenazine, methoulfate as photosensitizer. But 100ug oligomycin and 1mmol phlorizin ingibited activited activity of enzyme to 48% and 45%, respectively. Its optimum wavelength was 690nm on the effect of K ion influx, its optimum pH and temperature were found to be 7.2 and 55℃.
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