Purification, Properties and Reactivity of the Esterase form Micrococcus sp.

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概要

• 論文の詳細を見る

• The esterase form Micrococcus sp., which hydrolyzes n-propyl-2-fluorocyclopropanecarboxylate (3) enantioselectively, was highly purified by three types of chromatography. The purified enzyme was inactivated by Hg and diisopropyl fluorophosphate (DFP). It was a monomer with a molecular weight of about 35000. The enzyme exhibits esterase activity towards many aliphatic propyl esters. The enantioselectivity for substrate (3) using purified enzyme did not differ from that of crude enzyme.

• 公益社団法人日本薬学会の論文
• 1999-06-15

著者

• Itoh M

  Chemistry Laboratory Research Center Mochida Pharmaceutical Co. Ltd.

• MIYADERA Akihiko

  Chemical Technology Research Laboratories, Daiichi Pharmaceutical Co., Ltd.,

• IMURA Akihiro

  Chemical Technology Research Laboratories, Daiichi Pharmaceutical Co., Ltd.,

• Imura A

  Chemical Technology Research Laboratories Daiichi Pharmaceutical Co. Ltd.

• ITOH Motohiro

  Chemical Technology Research Laboratories, Daiichi Pharmaceutical Co., Ltd.,

• Miyadera A

  Chemical Technology Research Laboratories Daiichi Pharmaceutical Co. Ltd.

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