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      쥐 간의 카테콜 - O - 메칠전달 효소 : 정제 및 일반특성 = Rat Liver Catechol -O - Methyltransferase Purification and General properties

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      Catechol-O-methyltransferase (COMT; E. C. 2.1.1.6) from rat liver was purified and characterized. The purification steps involved acid precipitation, ammmonium sulfate fractionation, Sephadex G-100 gel filtration chromatography, and DEAF-cellulose ion-exchange chromatography. COMT was purified 147-fold with 23% recovery. On the SDS-PAGE, the final preparation showed one major band and a few minor bands. The K_m value of COMT for p-nitrocatechol was 3.8 μM and that for SAM was 283 μM. Magnesium ion was required for the optimal enzyme activity and the pH optimum was 7.8 with phosphate buffer. Maximum activity was exerted at 50℃. High ionic strength resulted in inactivation of the enzyme. The molecular weight was estimated as 25,700 by SDS-PAGE. When COMT was treated with a sulfhydryl group modifying reagent, iodoacetic acid, the inhibition of the enzyme activity was observed.
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      Catechol-O-methyltransferase (COMT; E. C. 2.1.1.6) from rat liver was purified and characterized. The purification steps involved acid precipitation, ammmonium sulfate fractionation, Sephadex G-100 gel filtration chromatography, and DEAF-cellulose ion...

      Catechol-O-methyltransferase (COMT; E. C. 2.1.1.6) from rat liver was purified and characterized. The purification steps involved acid precipitation, ammmonium sulfate fractionation, Sephadex G-100 gel filtration chromatography, and DEAF-cellulose ion-exchange chromatography. COMT was purified 147-fold with 23% recovery. On the SDS-PAGE, the final preparation showed one major band and a few minor bands. The K_m value of COMT for p-nitrocatechol was 3.8 μM and that for SAM was 283 μM. Magnesium ion was required for the optimal enzyme activity and the pH optimum was 7.8 with phosphate buffer. Maximum activity was exerted at 50℃. High ionic strength resulted in inactivation of the enzyme. The molecular weight was estimated as 25,700 by SDS-PAGE. When COMT was treated with a sulfhydryl group modifying reagent, iodoacetic acid, the inhibition of the enzyme activity was observed.

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