STUDIES ON TAKA-ACYLASE
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- INOUYE MASAYORI
- Laboratory of Biochemistry, Faculty of Science, Osaka University
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- KATO IKUNOSHIN
- Laboratory of Biochemistry, Faculty of Science, Osaka University
抄録
The activation of Taka-acylase by Co++ was invesigated kinetically. A scheme for the acylase reaction is proposed and it is concluded that Co++ mediates in the binding of the substrate to the enzyme and that with aromatic substrates such as ace tyl-L-phenylalanine, the enzyme-metal-substrate complex is stabilized by the interaction of the benzene ring of the substrate with a site of the enzyme. This is in contrast to the reaction with aliphatic substrates such as chloroacetyl-L-valine.<br> Inhibition by carboxylic acids and p-choloromercuribenzoate was also investigated kinetically.<br> A model of the active area of Taka-acylase is proposed and discussed.<br> The authors wish to express their deep gratitude to Dr. S. Akaboi, Prof. of Institute for Protein Research, for his kind guidance and Dr. Y. Ogura, Prof. of the University of Tokyo, for his valuable discussion throughout this investigation and also to Sankyo Co., Ltd. for kindly supplying “Taka-diastase Sankyo”.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 48 (5), 745-757, 1960
社団法人 日本生化学会
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詳細情報 詳細情報について
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- CRID
- 1570291228034962944
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- NII論文ID
- 130006876850
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles