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Abstract
Incubation at 70℃ 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.
Journal
- Bioscience, biotechnology, and biochemistry [List of Volumes]
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Bioscience, biotechnology, and biochemistry 65(3), 698-701, 2001-03-23 [Table of Contents]
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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