Results 41 to 50 of about 52 (52)
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Biochemistry, 1993
Quasielastic light scattering (QELS) measurements on several preparations of bovine heart and kidney pyruvate dehydrogenase complex yielded hydrodynamic radii (rH values) ranging from 25.7 to 30 nm. Gel filtration chromatography removed stable aggregates and generated preparations that gave essentially the same rH values of 24.3 +/- 0.6 nm for both ...
Thomas E. Roche +7 more
openaire +2 more sources
Quasielastic light scattering (QELS) measurements on several preparations of bovine heart and kidney pyruvate dehydrogenase complex yielded hydrodynamic radii (rH values) ranging from 25.7 to 30 nm. Gel filtration chromatography removed stable aggregates and generated preparations that gave essentially the same rH values of 24.3 +/- 0.6 nm for both ...
Thomas E. Roche +7 more
openaire +2 more sources
Biochemistry, 1983
We have characterized the dissociation equilibrium constant (Kd) and the rate constants of association and dissociation for the binding of the pyruvate dehydrogenase component (PDH) to the dihydrolipoyl transacetylase component of kidney pyruvate dehydrogenase complex.
Mary L. Pratt +2 more
openaire +3 more sources
We have characterized the dissociation equilibrium constant (Kd) and the rate constants of association and dissociation for the binding of the pyruvate dehydrogenase component (PDH) to the dihydrolipoyl transacetylase component of kidney pyruvate dehydrogenase complex.
Mary L. Pratt +2 more
openaire +3 more sources
Archives of Biochemistry and Biophysics, 1992
The pyruvate dehydrogenase complex (PDC) from muscle of the adult parasitic nematode Ascaris suum plays a unique role in its anaerobic mitochondrial metabolism. Resolution of the intact complex in high salt dissociates the pyruvate dehydrogenase subunit but leaves the dihydrolipoyl dehydrogenase subunit (E3) and two other proteins with apparent M(r)s ...
Richard Komuniecki +5 more
openaire +3 more sources
The pyruvate dehydrogenase complex (PDC) from muscle of the adult parasitic nematode Ascaris suum plays a unique role in its anaerobic mitochondrial metabolism. Resolution of the intact complex in high salt dissociates the pyruvate dehydrogenase subunit but leaves the dihydrolipoyl dehydrogenase subunit (E3) and two other proteins with apparent M(r)s ...
Richard Komuniecki +5 more
openaire +3 more sources
European Journal of Biochemistry, 1991
Site‐directed mutagenesis was performed in the protease‐sensitive region, between the lipoyl and catalytic domains and in the catalytic domain, of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Adrie H. Westphal +3 more
openaire +3 more sources
Site‐directed mutagenesis was performed in the protease‐sensitive region, between the lipoyl and catalytic domains and in the catalytic domain, of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
Adrie H. Westphal +3 more
openaire +3 more sources
European Journal of Biochemistry, 1991
Partial sequences of the dihydrolipoyl transacetylase componenent (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli, containing the catalytic domain, were cloned in pUC plasmids and over‐expressed in E. coli TG2.
Schulze E +5 more
openaire +5 more sources
Partial sequences of the dihydrolipoyl transacetylase componenent (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli, containing the catalytic domain, were cloned in pUC plasmids and over‐expressed in E. coli TG2.
Schulze E +5 more
openaire +5 more sources