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Purification and Characterization of Tyrosinase from Solanum melongena
Lee, Jong-Liong,Kong, Kwang-Hoon,Cho, Sung-Hye Korean Society for Biochemistry and Molecular Biol 1997 Journal of biochemistry and molecular biology Vol.30 No.2
Tyrosinase was purified from Solanum melongena by ammonium sulfate precipitation, Sephadex G-150 and DEAE-Sephacel column chromatography. The molecular weight of the purified tyrosinase was approximately 88,600 daltons with 805 amino acid residues. The amino acid composition showed the characteristic high contents of glycine, glutamic acid and serine residues. The enzyme had high substrate specificity towards (+)-catechin. The $K_m$, value for L-DOPA was 20.8 mM. L-ascorbic acid, ${\beta}-mercapto-ethanol$, sodium diethyldithiocabamate, KCN and $NaN_3$ had strong inhibitory effects on enzyme activity. Sodium diethyldithiocabamate was a competitive inhibitor of the enzyme with a $K_i$ value of $5.2{\times}10^{-2}\;mM$. The optimum pH of the enzyme was 9.0 and the optimum temperature was $65^{\circ}C$ with L-DOPA as a substrate. In addition, the activity was enhanced by addition of $Ca^{+2}$ or $Cu^{+2}$, but decreased in the presence of $Fe^{2+},Fe^{3+}$ and $Zn^{2+}$ ions.
조성희,이종용 中央大學校 基礎科學硏究所 1993 基礎科學硏究所 論文集 Vol.7 No.-
It was observed biochemical changes and germination rate of capsicum annuum L. Var acuminatum FING. seeds treated by GA₃(500ppm. 100ppm, 50ppm) during germination stages. The result were as follows: 1. The content of soluble glucose of seeds treated by GA₃was increased and remarkably increased by the light. 2. The content of soluble protein of seeds treated by GA₃was decreased as compared with eighth days of control in Dark and Light. 3. The Trehalase activity of seeds treated by GA₃was increased and remarkably increased by the Light. 4. The more GA₃was much, the more germination rate was remarkably increased as compared with control during germination stages in Dark and Light.
Purification and Characterization of Tyrosinase from Solanum melongena
Cho, Sung Hye,Kong, Kwang Hoon,Lee, Jong Liong 생화학분자생물학회 1982 BMB Reports Vol.30 No.2
Tyrosinase was purified from Solanum melongena by ammonium sulfate precipitation, Sephadex G-150 and DEAF-Sephacel column chromatography. The molecular weight of the purified tyrosinase was approximately 88,600 daltons with 805 amino acid residues. The amino acid composition showed the characteristic high contents of glycine, glutamic acid and serine residues. The enzyme had high substrate specificity towards (+)-catechin. The K_m value for L-DOPA was 20.8 mM. L-ascorbic acid, β-mercaptoethanol, sodium diethyldithiocabamate, KCN and NaN₃ had strong inhibitory effects on enzyme activity. Sodium diethyfdithiocabamate was a competitive inhibitor of the enzyme with a K_i value of 5.2 × 10^(-2) mM. The optimum pH of the enzyme was 9.0 and the optimum temperature was 65㎖ with L-DOPA as a substrate. In addition, the activity was enhanced by addition of Ca^(2+) or Cu^(2+), but decreased in the presence of Fe^(2+), Fe^(3+) and Zn^(2+) ions.