Thermal Disassembly of Pyruvate Dehydrogenase Multienzyme Complex from Bacillus stearothermophilus

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概要

• 論文の詳細を見る

• Thermostabilities of component enzymes in the pyruvate dehydrogenase complex from Bacillus stearothermophilus decreased in the order lipoamide dehydrogenase, lipoate acetyltransferase, and pyruvate decarboxylase (E1). Fluorescence of an extrinsic 8-amino-1-naphthalenesulfonate (ANS) increased with inactivation of E1. The thermal denaturation of the enzymes resulted in disassembly of the complex. E1 was involved in a resulting aggregate of the complex. The interaction between ANS and denatured E1 accounted for an increase in fluorescence.

• 1994-10-23

著者

• ASO yoichi

  Laboratory of Protein Chemistry & Engineering, Kyushu University

• Yamashita Shoji

  Faculty Of Agriculture Graduate School Of Kyushu Univ

• Aso Y

  Institute Of Genetic Resources Graduate School Of Bioresources And Bioenvironmental Science Kyushu U

• Yamashita S

  Institute Of Biophysics Faculty Of Agriculture Graduate School Of Kyushu University

• YAMASHITA Shoji

  Laboratory of Biophysics, Faculty of Agriculture, Kyushu University

• Hiromasa Yasuaki

  Laboratory Of Protein Chemistry And Engineering Department Of Genetic Resources Technology Graduate

• ASO Yoichi

  Laboratory of Genetic and Protein Engineering, Faculty of Agriculture, Kyushu University

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