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＜departmental bulletin paper＞
Denaturation of the Bacillus stearothermophilus Dihydrolipoamide Dehydrogenase in the Presence of Guanidine-HCl at Low Temperature

Creator
Author PID
K005220
Creator Name
Hiromasa, Yasuaki
廣政, 泰明
ヒロマサ, ヤスアキ
Affiliation
Affiliation Name
Laboratory of Protein Chemistry and Engineering, Department of Genetics Resources Technology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
Creator Name
Meno, Kohji
目野, 高嗣
メノ, コウジ
Affiliation
Affiliation Name
Laboratory of Protein Chemistry and Engineering, Department of Genetics Resources Technology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University
Author PID
K001565
Creator Name
Aso, Yoichi
麻生, 陽一
アソウ, ヨウイチ
Language
English
Publisher
Faculty of Agriculture, Kyushu University
九州大学大学院農学研究院
Date
2003-02-01
Source Title
Journal of the Faculty of Agriculture, Kyushu University
Vol
47
Issue
2
First Page
387
Last Page
394
Publication Type
Version of Record
Access Rights
open access
Crossref DOI
https://doi.org/10.5109/4509
Related DOI
Journal of the Faculty of Agriculture, Kyushu University || 47(2) || p387-394
九州大学大学院農学研究院紀要 || 47(2) || p387-394
http://www.agr.kyushu-u.ac.jp/index.html
Related URI
Journal of the Faculty of Agriculture, Kyushu University || 47(2) || p387-394
九州大学大学院農学研究院紀要 || 47(2) || p387-394
http://www.agr.kyushu-u.ac.jp/index.html
Relation
Journal of the Faculty of Agriculture, Kyushu University || 47(2) || p387-394
九州大学大学院農学研究院紀要 || 47(2) || p387-394
http://www.agr.kyushu-u.ac.jp/index.html

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Details

PISSN
0023-6152
NCID
AA00697606
Record ID
4509
Peer-Reviewed
Unrefereed
ISSN
0023-6152
NCID
AA00697606
Notes
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.
Created Date 2009.04.22
Modified Date 2022.11.11

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