The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Guanidine Hydrochloride-Induced Changes of the E2 Inner Core of the Bacillus stearothermophilus Pyruvate Dehydrogenase Complex
Yasuaki HiromasaYoichi AsoKouta MayanagiYorinao InoueTetsuro FujisawaKohji MenoTatzuo Ueki
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1998 Volume 123 Issue 4 Pages 564-567

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Abstract

The limited proteolysis of the Bacillus stearothermophilus pyruvate dehydrogenase complex by V8 protease yields its core structure solely composed of lipoate acetyltransferase (E2) fragments. The changes in the core with guanidine hydrochloride (GdnHCl) were biphasic: below 0.8 M (first) and above 1.0 M (second) GdnHCl. The changes in the first phase were slight but significant: decreases in ellipticity and light scattering, and an increase in E2 activity. Insignificant changes in the molecular shape and size of the core were detected on fluorescence spectroscopy, ultracentrifugation, gel filtration, and electron microscopy. On the other hand, the changes in the second phase were drastic; the core was disassembled and denatured.

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© The Japanese Biochemical Society
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