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버섯(Lentinus edodes(Berk)Sing) 중의 ATPase에 관한 연구(Ⅰ)
민태진,박혜련 동국대학교 자연과학연구소 1986 자연과학연구 논문집 Vol.6 No.-
표고버섯, Lentinus edodes(Berk) Sing 중의 ATPase를 (NH₄)₂SO₄분별침전 및 Sephadex G-200겔 여과로 정제하였다. 이버섯 중에서 세 종류의 단백질 분획을 얻었으며, adenosine-5'-triphosphate기질에 대한 두 종류의 활성분획 Ⅰ과 Ⅱ를 얻었다. 이 효소는 활성도의 최적 pH는 7.6이었고, 최적온도는 58℃, 열 안정성은 20℃~40℃였다. SDS-PAGE dalton에 의해 측정한 이 효소는 겉보기 분자량은 74,000 dalton이었다. ATPase in the L. edodes was purified by 30% ammonium sulfate saturation and for ? times, by Sephadex G-200 gel filtration chromatography. Three kinds fo rotein fractions were isolated from this mushroom and fraction Ⅰ and Ⅱ showed its activity toward substrate adenosine5-triphoshgate(ATP) Its optimum pH and optimum temperature were found to be pH 7.6 and 58℃, its thermal stabililty was 20℃~40℃. Apparent molecular weight of ATPase was determinded to be 74,000 dalton by SDS-PAGE.
민태진,박혜련 한국균학회 1991 韓國菌學會誌 Vol.19 No.3
Activities of the F₁-ATPase purified from Lentinus edodes were stimulated by Fe^(2+), Fe^(2+), Cd^(2+), Mg^(2+), K^+ and Co^(2+) but were inhibited by Zn^(2+), Ca^(2+), Cu^(2+) and Ni^(2+) ion. The enzyme activities were increased 130, 65, 65, 68, 105% and 23% by the 5 mM Fe^(3+), 10 mM Fe^(2+), 1 mM Cd^(2+), 5 mM Mg^(2+), 5 mM K^+ and 5 mM Co^(2+) ion addition, respectively, as compared with those not added. The enzyme activities were decreased 18, 19, 27 and 30% by 10 mM Zn^(2+), 10 mM Ca^(2+), 0.5 mM C^(2+) and 10 mM Ni^(2+) ion, respectively. .onion effects of 10 mM CO₃^(2+), 20 mM CN^-, 20 mM CH₃COO^- and 20 mM NO₃^- ion were inhibited to the enzyme activities of 98, 95, 70 and 50%, respectively. As increasing of SO₄^(2+) ion concentration, the enzyme activity was stimulated and 20 mM SO₄^(2+) ion was shown increased of 21%.
민태진,박혜련,배강규 ( Tae Jin Min,Hye Lyoun Park,Kang Gyu Bae ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.4
The activities of purified ATPase in L. edodes were inhibited by 1-fluoro-2,4-dinitrobenzene (FDNB), N,N`-dicyclohexylcarbodiimide(DCCD), ethacrynic acid(EA) and carbonylcyanide mchlorophenylhydrazone(CCCP), but were stimulated by succinic acid(SA), ninhydrin(NH), iodoacetic acid(IA) and picric acid(PA). The enzyme activities were inhibited 89%, 37%, 19%, and 15% by 0.4 mM FDNB, 0.3 mM DCCD, 0.2 mM EA and 0.15 mM CCCP, but stimulated 51%, 21%, 14% and 15% by 1.5 mM SA, 0.01 mM NH, 0.5 mM IA and 1.0 mM PA, respectively. By amino acid having the ring formed hydrophobic residues (0.1 mM proline, 0.1 mM tryptophan and 1.5 mM phenylalanine) increased the enzyme activities up to 17%, 8% and 20% but were decreased 45% and 48% by amino acids having hydrophobic and aliphatic residues (0.8 mM norleucine and 2.5 mM isoleucine), respectively. And positively charged amino acid of 1.5 mM histidine inhibited 21% of enzyme activity, negatively charged amino acid of aspartic acid did not affected. Also polared but uncharged amino acids (1.5 mM cysteine and 1.0 mM serine) increased 25% and 27% of enzyme activities, but 0.01 mM tyrosine having a hydroxyphenyl residue inhibited 50% of enzyme activity.