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      저자 : 최명언 ( Jie Oh Lee (검색결과 2 건)
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        쥐 뇌의 용해단백질 황산기 전달효소의 식별과 부분특성 연구

        이지오,최명언 ( Jie Oh Lee,Myung Un Choi ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.1

        Protein sulfotransferase (S) in soluble fraction of rat bran were characterized using [^(35)S] phosphoadenosinephosphosulfate (PAPS) as sulfate donor. [^(35)S] PAPS, the universal sulfate donor, was prepared enzymatically in rat liver high speed supernatant with carrier free ^(35)S0₄ and ATP. The activity of soluble protein sulfotransferase was observed in assay system containing [^(35)S] PAPS, Tris-maleate buffer pH 6.7 and soluble proteins from rate brain. The sulfated proteins were separated by SDS-PAGE and acid treatment was performed on the gel to differentiate tyrosine sulfate from carbohydrate sulfate. Incorporation of sulfate into tyrosine residues of proteins of various molecular weights was observed. Particularly high molecular weight ($gt;200 kD) proteins were more intensively sulfated. Effects of incubation time, temperature, pH, amounts of proteins, PAPS concentration, various metal ions, and some polyamino acids on the activities of protein sulfotransferases were investigated. These general properties of the soluble sulfotransferase were mostly distinct from those of the microsome associated sulfotransferase.

      • SCIESCOPUSKCI등재

        쥐 뇌의 용해단백질 황산기 전달효소의 식별과 부분특성 연구

        최명언,이지오 생화학분자생물학회 1993 BMB Reports Vol.17 No.3

        Protein sulfotransferase (S) in soluble fraction of rat bran were characterized using [^(35)S] phosphoadenosinephosphosulfate (PAPS) as sulfate donor. [^(35)S] PAPS, the universal sulfate donor, was prepared enzymatically in rat liver high speed supernatant with carrier free ^(35)S0₄ and ATP. The activity of soluble protein sulfotransferase was observed in assay system containing [^(35)S] PAPS, Tris-maleate buffer pH 6.7 and soluble proteins from rate brain. The sulfated proteins were separated by SDS-PAGE and acid treatment was performed on the gel to differentiate tyrosine sulfate from carbohydrate sulfate. Incorporation of sulfate into tyrosine residues of proteins of various molecular weights was observed. Particularly high molecular weight ($gt;200 kD) proteins were more intensively sulfated. Effects of incubation time, temperature, pH, amounts of proteins, PAPS concentration, various metal ions, and some polyamino acids on the activities of protein sulfotransferases were investigated. These general properties of the soluble sulfotransferase were mostly distinct from those of the microsome associated sulfotransferase.

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