매미나방(Lymantria dispar)의 혈림프 exo-$\\beta$-N-acetylglucosaminidase 2의 정제와 특성 Purification and Characterization of Haemolymph exo-$\\beta$-N-Acetylglucosaminidase 2 from Lymantria dispar
매미나방 (Lymantria dispar)에서 4종의 $eta$-N-acetylglucosaminidase를 확인하였으며 이 중 exo-$\beta$-N-acetylglucosaminidase 2(E2)를 column chromatography에 의해 분리, 정제하였다. 분자량은 27Kda, pI는 5.75, $ho$-nitrophenyl-N-acetyl-$\beta$-D-glucosamine에 대한 Km 값은 2.5$\times$$10^{-3}$M이었다. 또한 최적반응 pH는 5.5. 최적반응 온도는 7$0^{\circ}C$이었으며, 7$0^{\circ}C$까지 열안정성을 나타내었으나 그 이후 급격히 활성이 소실되었다. 정제된 효소는 $Mg^{2+}$, $Mn^{2+}$, $Ca^{2+}$, $K^{+}$ 등에 의해 활성이 증가되었으며 반면에 H $g^{2+}$, C $u^{2+}$, F $e^{2+}$, F $e^{3+}$ 등에 의해 활성이 억제되었다.다.
매미나방 (Lymantria dispar)에서 4종의 $eta$-N-acetylglucosaminidase를 확인하였으며 이 중 exo-$\beta$-N-acetylglucosaminidase 2(E2)를 column chromatography에 의해 분리, 정제하였다. 분자량은 27Kda, pI는 5.75, $ho$-nitrophenyl-N-acetyl-$\beta$-D-glucosamine에 대한 Km 값은 2.5$\times$$10^{-3}$M이었다. 또한 최적반응 pH는 5.5. 최적반응 온도는 7$0^{\circ}C$이었으며, 7$0^{\circ}C$까지 열안정성을 나타내었으나 그 이후 급격히 활성이 소실되었다. 정제된 효소는 $Mg^{2+}$, $Mn^{2+}$, $Ca^{2+}$, $K^{+}$ 등에 의해 활성이 증가되었으며 반면에 H $g^{2+}$, C $u^{2+}$, F $e^{2+}$, F $e^{3+}$ 등에 의해 활성이 억제되었다.다.
Four isozymes of $\beta$-N-acetylglucosaminidase were found in gypsy moth Lympantria dispar. Of these isozymes exo-$\beta$-N-acetylglucosaminidase 2 (E2) was isolated and purified by different types chromatography E2 had a molecular weight of 27 Kda, an isoelectric point of 5.7...
Four isozymes of $\beta$-N-acetylglucosaminidase were found in gypsy moth Lympantria dispar. Of these isozymes exo-$\beta$-N-acetylglucosaminidase 2 (E2) was isolated and purified by different types chromatography E2 had a molecular weight of 27 Kda, an isoelectric point of 5.75 and a Km value of 2.5$\times$10$^{-3}$ M. The optimum pH and temperature of the enzyme were pH 5.5 and 7$0^{\circ}C$, respectively, and maintained its normal activity until 7$0^{\circ}C$. E2 was activated by $Mg^{2+}$, M $n^{2+}$, $Ca^{2+}$ and $K^{+}$, and inhibited by H $g^{2+}$, C $u^{2+}$, F $e^{2+}$, F $e^{3+}$./.+}$./.
Four isozymes of $\beta$-N-acetylglucosaminidase were found in gypsy moth Lympantria dispar. Of these isozymes exo-$\beta$-N-acetylglucosaminidase 2 (E2) was isolated and purified by different types chromatography E2 had a molecular weight of 27 Kda, an isoelectric point of 5.75 and a Km value of 2.5$\times$10$^{-3}$ M. The optimum pH and temperature of the enzyme were pH 5.5 and 7$0^{\circ}C$, respectively, and maintained its normal activity until 7$0^{\circ}C$. E2 was activated by $Mg^{2+}$, M $n^{2+}$, $Ca^{2+}$ and $K^{+}$, and inhibited by H $g^{2+}$, C $u^{2+}$, F $e^{2+}$, F $e^{3+}$./.+}$./.
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