Sulfation of Parabens and Tyrosylpeptides by Bacterial Arylsulfate Sulfotransferases
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概要
- 論文の詳細を見る
Arylsulfate sulfotransferase purified from Eubacterium A-44 has higher specific activity than the enzymes from Klebsiella K-36 and Haemophilus K-12. Propylparaben and butylparaben were good substrates among several parabens. The antibacterial activity of parabens was reduced by the sulfation of the phenolic hydroxy group. Tyrosine-containing peptides, kyotorphin, enkephalin and cholecystokinin non-sulfate, were effective as acceptor substrates by A-44,K-36 and K-12 sulfotransferases.
- 社団法人日本薬学会の論文
- 1994-10-15
著者
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小橋 恭一
Faculty Of Pharmaceutical Sciences Toyama Medical And Pharmaceutical University
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金 東鉉
College Of Pharmacy Kyung-hee University
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金 東鉱
College Of Pharmacy Kyunghee University
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KIM HyungSoo
College of Pharmacy, Kyunghee University
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KIM Byungtaek
College of Pharmacy, Kyung-Hee University
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SOHNG InSeok
College of Pharmacy, Kyung-Hee University
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Kobayashi K
Faculty Of Pharmaceutical Sciences Toyama Medical And Pharmaceutical University
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Sohng Inseok
College Of Pharmacy Kyung-hee University
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Kim Hyungsoo
College Of Pharmacy Kyung-hee University
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Kim Byungtaek
College Of Pharmacy Kyung-hee University
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