TY - JOUR
T1 - Guanidine hydrochloride-induced changes of the E2 inner core of the Bacillus stearothermophilus pyruvate dehydrogenase complex
AU - Hiromasa, Yasuaki
AU - Aso, Yoichi
AU - Mayanagi, Kouta
AU - Inoue, Yorinao
AU - Fujisawa, Tetsuro
AU - Meno, Kohji
AU - Ueki, Tatzuo
PY - 1998/1/1
Y1 - 1998/1/1
N2 - 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.
AB - 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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U2 - 10.1093/oxfordjournals.jbchem.a021973
DO - 10.1093/oxfordjournals.jbchem.a021973
M3 - Article
C2 - 9538243
AN - SCOPUS:0031966058
VL - 123
SP - 564
EP - 567
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 4
ER -