A New Type of Streptomycete Arylsulfatase with High Affinity to the Sulfuryl Moiety of the Substrate
スポンサーリンク
概要
- 論文の詳細を見る
Streptomyces sp. T109-3 arylsulfatase (Es-2), which desulfated p-nitrophenyl sulfate as well as etoposide 4'-sulfate, was purified to protein homogeneity by sulfated cellulose affinity and DEAE-cellulose column chromatographies. Es-2 required calcium for enzyme activity and was severely inhibited by SH and chelating reagents. Comparative characterization showed that, although distinct in recognition of the binding moiety of substrate, Es-1 (Streptomyces griseorubiginosus S980-14 arylsulfatase) and Es-2 shared high desulfating activity on etoposide 4'-sulfate and many other common enzymological characteristics, which suggested they would be acceptable as the enzyme component of antitumor antibody-enzyme conjugates for target chemotherapy.
- 社団法人日本農芸化学会の論文
- 1995-06-23
著者
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Sawada Y
Dept. Of Appl. Biol. Sci. Nihon University:(present Office)riken Psc
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Ueki Tomokazu
Bristol-Myers Squibb Research Institute
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Sawada Yosuke
Bristol-Myers Squibb Research Institute
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Fukagawa Yasuo
Bristol-Myers Squibb Research Institute
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Oki Toshikazu
Bristol-Myers Squibb Research Institute
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Oki Toshikazu
Bristol-myers Squibb Research Institute Ltd. Tokyo Research Center
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Fukagawa Yasuo
Bristol-myers Squibb Research Institute Ltd. Tokyo Research Center
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Fukagawa Yasuo
Central Research Laboratories Sanraku Incorporated
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Sawada Y
Bristol-myers Squibb Research Institute:funakoshi Co. Ltd. Life Science Products Division
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