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RISS 인기검색어
- 검색키워드
- 저자 : 최명언 ( Che Hun Jung (검색결과 4 건)
- 무료
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Immobilization of Rat Brain Arylsulfatase A on Sepharose 4B
정제훈,최명언,Jung, Che-Hun,Choi, Myoung-Un 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.4
브롬화 시안으로 활성화시킨 Sepharose 4B에 쥐 뇌로부터 정제한 arylsulfatase A단량체를 고정화시켰다. 효소의 99%까지 고정화 시킬 수 있었으며 본래의 효소와 고정화된 효소의 일반적 성질을 비교하였다. 고정후에도 효소활성이 잘 보존되었으며, Km 값의 증가 및 pH와 열에 대한 효소안정도의 향상이외에는 효소의 일반적 성질은 거의 변하지 않았다. 이는 Sepharose 4B에 공유결합으로 고정되는 효소의 활성부위가거의 영향을 받지 않고 있음을 나타낸다. 특히 고정화된 효소도 수소이온 농도변화에 따른 최적점이 두 개로 나타나는데, 이는 단량체-이량체 결속현상으로 만은 설명되지 못함을 암시해주고 있다. Rat brain arylsulfatase A monomer was immobilized to CNBr-activated Sepharose 4B. The coupling of the enzyme could be accomplished up to the degree of 99%. The general properties of the immobilized arylsulfatase A were compared with those of the soluble enzyme. The enzymatic activity of the enzyme was conserved well by immobilization and the catalytic properties of the immobilized enzyme were similar to the soluble one except the increased Km value and the improvement of stabilities toward heat and pH. Thus the covalent coupling of the enzyme to Sepharose 4B did not affect vitally the functional groups of the active site of the enzyme. The two-pH optima profile of the immobilized enzyme imply that the multiple pH optima of the arylsulfatase A could not be explained solely by the monomer-dimer association.
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쥐 뇌의 아릴설파타아제 A 의 Sepharose 4B에의 고정화
정제훈,최명언 ( Che Hun Jung,Myung Un Choi ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.4
Rat brain arylsulfatase A monomer was immobilized to CNBr-activated Sepharose 4B. The coupling of the enzyme could be accomplished up to the degree of 99%. The general properties of the immobilized arylsulfatase A were compared with those of the soluble enzyme. The enzymatic activity of the enzyme was conserved well by immobilization and the catalytic properties of the immobilized enzyme were similar to the soluble one except the increased Km value and the improvement of stabilities toward heat and pH. Thus the covalent coupling of the enzyme to Sepharose 4B did not affect vitally the functional groups of the active site of the enzyme. The two-pH optima profile of the immobilized enzyme imply that the multiple pH optima of the arylsulfatase A could not be explained solely by the monomer-dimer association.
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안경숙,정제훈,최명언 ( Kyoung Sook Ann,Che Hun Jung,Myung Un Choi ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.4
Arylsulfatases A (arylsulfate sulfohydrolase, EC 3.1.6.1) from rat brain was separated and purified 90-fold with 7% recovery. The purification steps involved ammonium sulfate fractionation, DEAE-Cellulose ion exchange chromatography, concanavalin A-Sepharose 4B affinity chromatography and gel filtration on Sephadex G-200. The specific activity of arylsulfatase A with p-nitrocatechol sulfate as substrate was 6.8 μ㏖/min/㎎ protein. Arylsulfatase A had two pH optima, pH 5.2 and 5.8, and the molecular weight of the enzyme was estimated to 120,000 by gel filtration on Sephadex G-200 at pH 7.4. The arylsulfatase A undergoes self-association to dimeric form with molecular weight of 230,000 at pH 4.5. In order to verify the catalytic groups of arylsulfatase A, the effects of the various chemical reagents for protein modification were tested. It was observed that the enzyme was inactivated by phenylglyoxal, N-ethyl-maleimide, p-chloromercuribenzoate, and 1-ethyl-3(dimethylaminopropyl)carbodiimide.
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Isolation and Characterization of Arylsulfatase A from Rat Brain
안경숙,정제훈,최명언,Ann, Kyoung-Sook,Jung, Che-Hun,Choi, Myung-Un 생화학분자생물학회 1987 한국생화학회지 Vol.20 No.4
Arylsulfatases A (arylsulfate sulfohydrolase, EC 3.1.6.1) from rat brain was separated and purified 90-fold with 7% recovery. The purification steps involved ammonium sulfate fractionation, DEAE-Cellulose ion exchange chromatography, concanavalin A-Sepharose 4B affinity chromatography and gel filtration on Sephadex G-200. The specific activity of arylsulfatase A with p-nitrocatechol sulfate as substrate was $6.8\;{\mu}mole/min/mg$ protein. Arylsulfatase A had two pH optima, pH 5.2 and 5.8, and the molecular weight of the enzyme was estimated to 120,000 by gel filtration on Sephadex G-200 at pH 7.4. The arylsulfatase A undergoes self-associati on to dimeric form with molecular weight of 230,000 at pH 4.5. In order to verify the catalytic groups of arylsulfatase A, the effects of the various chemical reagents for protein modification were tested. It was observed that the enzyme was inactivated by phenylglyoxal, N-ethylmaleimide, p-chloromercuribenzoate, and 1-ethyl-3(dimethylaminopropyl)carbodiimide. 아릴설파타아제 A를 쥐의 뇌로부터 분리하여 $(NH_4)_2SO_4$침전, DEAE-셀룰로즈, Con A-Sepharose 4B 크로마토크래피 및 Sephadex G-200 젤 여과법으로 7%의 회수율로 90배 정제하였다. 기질로서 p-nitrocatechol sulfate를 사용하였을 때 정제된 아릴설파타아제 A의 활성도는 $6.8\;{\mu}mole/min/mg$ protein이였으며, $K_m$과 $V_{max}$값은 각각 0.6 mM과 $7.1\;{\mu}mole/min/mg$ protein이었다. 효소 활성의 최적 pH는 pH 5.2와 5.8이며 아릴설파타아제 A의 분자량은 젤 여과법으로 pH 7.4에서 120,000으로 나타났다. 아릴설파타아제 A는 pH 4.5에서 두 분자가 결합하여 분자량 230,000의 이합체를 형성하였다. 이 효소의 촉매에 참여하는 group를 밝히기 위해 각종 단백질 개조용 시약들을 검토했다. 이둘중 phenylglyoxal, N-ethyl-maleimide, p-chloromercuribenzoate 및 1-ethyl-3(dimethylaminopropyl)carbodiimide는 효소를 효과적으로 저해시키는 것으로 관찰되었다.
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