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- 저자 : 양철학 ( In Hwan Hwang (검색결과 4 건)
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Arylsulphatases B and Bm from Rat Uterus: Their Purifications and Characterizations
황인환,양철학,Hwang, In-Hwan,Yang, Chul-Hak 생화학분자생물학회 1984 한국생화학회지 Vol.17 No.2
아릴썰파타아제 B 및 Bm(아렬썰페이트 썰포하이드롤라아제 ; E.C.3.1.6.1)이 쥐의 자궁으로부터 분리되고 그 특성이 연구되었다. 아릴썰파타아제 B는 286배로 정제되고 그 수율은 23%이었으며 Bm은 112배 정제되고 그 수율은 5.4%이었다. 통판 전기영동에 의해 마지막으로 얻어진 아릴썰파타아제 B 및 Bm은 하나의 단백질 띠로 나타났다. 이 효소들은 파라-나이트로카테콜썰페이트를 기질로 사용했을 때 정상적인 시간-활동도의 관계를 나타냈다. $K_m$과 $V_{max}$ 값은 아릴썰파타아제 B가 $2.0{\times}10^{-3}M$ 및 20.8 nmol/min 이었고 아릴썰파타아제 Bm은 $3.9{\times}10^{-3}M$ 및 67 nmol/min 이었다. 쥐의 자궁은 상당한 양의 음성형의 아릴썰파타아제 B(즉 아릴썰파타아제 Bm)를 함유하고 있었다. 아릴썰파타아제 Bm은 물리화학적 성질 가운데서 pH 적정점, 열에 대한 안정도, 썰페이트, 썰파이트 및 포스페이트에 대한 방해작용이나 시간-활동도의 관계에 있어 아릴썰파타아제 B와 거의 비슷한 결과를 나타냈다. Arylsulphatases B and Bm (arylsulphate sulphohydrolase; E.C.3.1.6.1) from rat uterus were purified and characterized. Arylsulphatases B and Bm were purified 286-fold and 1I2-fold with an overall recovery 23% and 5.4%, respectively. On disc gel electrophoresis, both final preparations of arylsulphatases B and Bm showed one protein band. These enzymes showed normal time-activity relationship with p-nitrocatechol sulphate as substrate. The $K_m$ and $V_{max}$ values were $2.0{\times}10^{-3}\;M$ and 20.8 nmol/min for arylsulphatase Band $3.9{\times}10^{-3}\;M$ and 67 nmol/min for arylsulphatase Bm, respectively. Rat uterus contained significant quantities (16~20% of total arylsulphatase) of an anionic form of arylsulphatase B (arylsulphatase Bm). The physico-chemical properties of arylsulphatase Bm were very similar to those of arylsulphatase B with respect to pH optimum, heat stability, the types of inhibition by sulphate, sulphite and phosphate ions, molecular weight, temperature optimum, and time-activity relationship.
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Purification and Characterization of Arylsulfatase A from Rat Uterus
황인환,양철학,Hwang, In-Hwan,Yang, Chul-Hak 생화학분자생물학회 1983 한국생화학회지 Vol.16 No.1
$(NH_4)_2\;SO_4$, 분획분리, DEAE-셀룰로즈 크로마토그라피, Sephadex G-200젤 여과법, Con A-Sepharose 흡착크로마토그라피 및 Sephadex G-200젤 여과법등을 이용하여 쥐의 자궁에서 아럴썰파타아제 A를 거의 순수한 상태로 정제하였다. 아랄쎌파타아제 A는 DEAE-셀룰로즈 column에 의하여 아릴썰파타아제 B와 Bm으로부터 분리되어졌고, DEAE-셀룰로즈 column으로 부터 0.2M NaCl 선형 농도증가에 의해서 흘러나왔다. 이 효소는 마지막 단계의 회수율이 8%였으며, 207배 정제되어졌으나 Disc-폴리아크릴아마이드 젤 영동법에 의하여 단일 단백질로 정제되지는 않았다. 아릴쎌파다아제 A는 비정상적인 시간에 따른 활동도 곡선을 나다냈다. 아릴썰파타아제 A는 $37^{\circ}C$에서 10 분동안의 반응에서는 pH 적정점은 pH 5.2와 pH 5.6이었는데, 60분 동안의 반응에서는 pH 5.0과 pH 5.6으로 바뀌어졌다. ${SO_4}^{2-}$, ${SO_3}^{2-}$ 및 ${PO_4}^{2-}$는 강한 방해제로서 작용하며 그들의 Ki값은 각각 $4.3{\times}10^{-3}M$, $6.6{\times}10^{-5}M$ 및 $3.0{\times}10^{-5}M$이었다. $P_2{O_7}^{2-}$와 $Cu^{2+}$ 이온은 아릴쎌파다아제 A 활성도를 방해하였으나 $Mn^{2+}$, $Co^{2+}$, $Ca^{2+}$와 ascorbic acid는 활성도를 오히려 증가시켰다. 반면에 $Ag^+$와 $Cl^-$이온은 효소의 활동에 전혀 영향을 미치지 않았다. 효소의 활성도는 $60^{\circ}C$까지 온도의 증가에 따라 계속 증가되 었으며 70분 동안 $60^{\circ}C$에서 82%의 활동도를 유지하였다. Sephadex G-200젤 여과법에 의하여 아랄쎌파타아제 A의 분자량은 pH 5.0 과 pH 7.2에서 모두 120,000 daltons으로 나타났다. Arylsulfatase A (aryl sulfate sulfohydrolase; E.C. 3.1.6.1) from rat uterus was highly purified by ammonium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 gel filtration. Conconavalin A-Sepharose affinity chramatography, and second gel filtration on Sephadex G-200. Arylsulfatase A was separated from arylsulfatases B and Bm by DEAE-cellulose column where arylsulfatase A was eluted at 0.2 M of NaCl linear gradient. The enzyme was purified 207-fold with 8% recovery, but disc polyacrylamide-gel electrophoresis showed that the purified preparation was not homogeneous. Arylsulfatase A showed the anomalous time-activity relationship. The $K_m$ and $V_{max}$ were 6.8 mM and 15.6 nmol/min, respectively. Arylsulfatase A had two pH optima at pH 5.2 and 5.6 for 10 min incubation time, and these optima shifted to pH 5.0 and 5.6 with incubation time of 60 min. ${SO_4}^{2-}$, ${SO_3}^{2-}$, and ${PO_4}^{2-}$ were strong inhibitors with Ki values of $4.3{\times}10^{-3}M$, $6.6{\times}10^{-5}M$, and $3.0{\times}10^{-5}M$, respectively. Pyrophosphate and $Cu^{2+}$ ion inhibited arylsulfatase A but $Mn^{2+}$, $Co^{2+}$, $Ca^{2+}$, and ascorbic acid activated the enzyme activity. Siver and $Cl^-$ ion did not affect the enzyme activity. Enzyme activity was increased to $60^{\circ}C$ for 10 min and thermally stable at $60^{\circ}C$ for 70 min with 82% of activity. By Sephadex G-200 gel filtration the molecular weight of arylsulfatase A was 120,000 at both pH 5.0 and 7.2.
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쥐의 자궁에서 아릴썰파타아제 A의 분리 및 그 성질에 관한 연구
황인환,양철학 ( In Hwan Hwang,Chul Hak Yang ) 생화학분자생물학회 1983 BMB Reports Vol.16 No.1
Arylsulfatase A (aryl sulfate sulfohydrolase; E.C. 3. 1. 6. 1) from rat uterus was highly purified by ammonium sulfate fractionation, DEAE-cellulose chromatography, Sephadex G-200 gel filtration. Conconavalin A-Sepharose affinity chramatography, and second gel filtration on Sephadex G-200. Arylsulfatase A was separated from arylsulfatases B and Bm by DEAE-cellulose column where arylsulfatase A was eluted at 0. 2 M of NaCl linear gradient. The enzyme was purified 207-fold with 8 % recovery, but disc polyacrylamide-gel electrophoresis showed that the purified preparation was not homogeneous. Arylsulfatase A showed the anomalous time-activity relationship. The K_m and V_(mas) were 6.8 mM and 15.6 nmol/min, respectively. Arylsulfatase A had two pH optima at pH 5. 2 and 5.6 for 10 min incubation time, and these optima shifted to pH 5.0 and 5.6 with incubation time of 60 min. SO₄^(2-), PO₄₃^(2-), and PO₄^(2-) were strong inhibitors with Ki values of 4.3×10^(-3)M, 6.6×10^(-5)M, and 3.0×10^(-6)M, respectively. Pyrophosphate and Cu^(2+) ion inhibited arylsulfatase A but Mn^(2+), Ca^(2+), Co^(2+), and ascorbic acid activated the enzyme activity. Siver and Cl- ion did not affect the enzyme activity. Enzyme activity was increased to 60 ℃ for 10 min and thermally stable at 60 ℃ for 70 min with 82 % of activity. By Sephadex G-200 gel filtration the molecular weight of arylsulfatase A was 120,000 at both pH 5.0 and 7.2.
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쥐의 자궁에서 아릴썰파타아제 B 및 Bm의 분리 및 그 효소의 특성에 관한 연구
황인환,양철학 ( In Hwan Hwang,Chul Hak Yang ) 생화학분자생물학회 1984 BMB Reports Vol.17 No.2
Arylsulphatases B and Bm (arylsulphate sulphohydrolase; E.C. 3.1.6.1) from rat uterus were purified and characterized. Arylsulphatases B and Bm were purified 286-fold and 112-fold with an overall recovery 23% and 5.4% respectively. On disc gel electrophoresis, both final preparations of arylsulphatases B and Bm showed one protein band. These enzymes showed normal time-activity relationship with p-nitrocatechol sulphate as substrate. The K_m and V_(max) values were 2.0×10^(-3) M and 20.8 nmol/min for arylsulphatase B and 3.9×10^(-3) M and 67 nmol/min for arylsulphatase Bm, respectively. Rat uterus contained significant quantities (16∼20% of total arylsulphatase) of an anionic form of arylsulphatase B (arylsulphatase Bm). The physico-chemical properties of arylsulphatase Bm were very similar to those of arylsulphatase B with respect to pH optimum, heat stability, the types of inhibition by sulphate, sulphite and phosphate ions, molecular weight, temperature optimum, and time-activity relationship.
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