Thermally induced changes of lipoate acetyltransferase inner core isolated from the Bacillus stearothermophilus pyruvate dehydrogenase complex
Incubation at 70°C converted the Bacillus stearothermophilus lipoate acetyltransferase inner core into an unidentified active molecular form, X, yielding an inactive aggregate. The core and X showed similar thermostabilities, but they were different in the recovery of enzyme activity after incubatio...
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Published in | Bioscience, biotechnology, and biochemistry Vol. 65; no. 3; pp. 698 - 701 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Tokyo
Japan Society for Bioscience, Biotechnology, and Agrochemistry
01.03.2001
Japan Society for Bioscience Biotechnology and Agrochemistry Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | Incubation at 70°C converted the Bacillus stearothermophilus lipoate acetyltransferase inner core into an unidentified active molecular form, X, yielding an inactive aggregate. The core and X showed similar thermostabilities, but they were different in the recovery of enzyme activity after incubation with 1.2-2.0 M guanidine hydrochloride and its subsequent removal; the core was hardly recovered, but X was well recovered. |
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Bibliography: | 2001004009 F60 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0916-8451 1347-6947 |
DOI: | 10.1271/bbb.65.698 |