Aso, Yoichi

Hiromasa, Yasuaki

Meno, Kohji

Denaturation of the Bacillus stearothermophilus dihydrolipoamide dehydrogenase induced by incubation with guanidine-HCl (GdnHCl) at 4℃ was examined. Enzyme activity was amplified by 2.5 times in 0.2M GdnHCl; such an increase in activity was also detected in NaCl and KCl at concentrations less than 1M, but not in urea. With increasing amount of GdnHCl, the enzyme lost half and all  its activity in 1.0M and 1.6M GdnHCl, respectively. Notable changes in fluorescence specta of Trp residue and FAD cofactor to the inactivation. Based on changes in fluerescence intensities and molecular ellipicity, a two-state transition equilibrium was suggested; transition midpoints were roughly at 1.7M GdnHCl at concentrations above 2M, the enzyme released FAD and formed inactive aggragate. Effects by GdnHCl at concentrations less than 1.4M were mostly chancelled by its removal. Most results were similar to those from studies on the enzyme being components of pyruvate dehdrogenase complex

廣政, 泰明

ヒロマサ, ヤスアキ

目野, 高嗣

メノ, コウジ

麻生, 陽一

アソウ, ヨウイチ

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Denaturation of the Bacillus stearothermophilus Dihydrolipoamide Dehydrogenase in the Presence of Guanidine-HCl at Low Temperature

Denaturation of the Bacillus stearothermophilus Dihydrolipoamide Dehydrogenase in the Presence of Guanidine-HCl at Low Temperature

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