Results 121 to 130 of about 22,770 (160)

Brain protein and α‐ketoglutarate dehydrogenase complex activity in alzheimer‐s disease

Annals of Neurology, 1996
AbstractTo determine whether the reduction in brain α‐ketoglutarate dehydrogenase complex activity in Alzheimer's disease (AD) is associated with an abnormality in one of its three constituent enzyme subunits, we measured protein levels of α‐ketoglutarate dehydrogenase (El), dihydrolipoamide succinyltransferase (E2), and dihydrolipoamide dehydrogenase (
Mastrogiacomo, Frank, Lindsay, J. Gordon, Bettendorff, Lucien, Rice, Jacqueline, Kish, Stephen J.   +4 more
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Role of excess lipoyl dehydrogenase in reconstituted α-ketoglutarate dehydrogenase complex of Escherichiacoli

Biochemical and Biophysical Research Communications, 1986
The alpha-ketoglutarate dehydrogenase complex of Escherichia coli can bind up to 12 dimers of dihydrolipoyl dehydrogenase (E3) besides those already present. Maximal activity does not increase, however, when surplus E3 is present. This observation was previously interpreted to mean that the excess enzyme is inactive.
T, Wagenknecht, N, Francis, D, DeRosier
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[12] α-ketoglutarate dehydrogenase complex from Escherichia coli

1969
Publisher Summary The chapter describes assay method, purification procedure, and properties of the α- ketoglutarate dehydrogenase enzyme. This enzyme has been isolated from pig heart muscle, Escherichia coli, and beef kidney mitochondria as multienzyme complexes with molecular weights of several million. The E.
Lester J. Reed, Barid B. Mukherjee
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An immunohistochemical study on α‐ketoglutarate dehydrogenase complex in Parkinson's disease

Annals of Neurology, 1994
AbstractWe report an immunohistochemical study of the mitochondrial α‐ketoglutarate dehydrogenase complex (KGDHC) in the substantia nigra in Parkinson's disease. The KGDHC, the three enzyme complex catalyzing the oxidation of α‐ketoglutarate to succinate through succinic semialdehyde, is the rate‐regulating enzyme of the TCA cycle.
Y, Mizuno, S, Matuda, H, Yoshino, H, Mori, N, Hattori, S, Ikebe   +5 more
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The alpha-ketoglutarate dehydrogenase complex.

Annals of the New York Academy of Sciences, 2000
The alpha-ketoglutarate dehydrogenase complex (KGDHC) is an important mitochondrial constituent, and deficiency of KGDHC is associated with a number of neurological disorders. KGDHC is composed of three proteins, each encoded on a different and well-characterized gene. The sequences of the human proteins are known. The organization of the proteins into
K F, Sheu, J P, Blass
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Brain α‐Ketoglutarate Dehydrotenase Complex Activity in Alzheimer's Disease

Journal of Neurochemistry, 1993
AbstractWe measured the activity of the a‐ketoglutarate dehydrogenase complex (α‐KGDHC), a rate‐limiting Krebs cycle enzyme, in postmortem brain samples from 38 controls and 30 neuropathologically confirmed Alzheimer's disease (AD) cases, in both the presence and absence of thiamine pyrophosphate (TPP), the enzyme's cofactor.
F, Mastrogiacomo, C, Bergeron, S J, Kish
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[Physiological function of alpha-ketoglutarate dehydrogenase complex in Torulopsis glabrata].

Wei sheng wu xue bao = Acta microbiologica Sinica, 2010
We studied the physiological function of alpha-ketoglutarate dehydrogenase complex (KGDH) on the metabolism of Torulopsis glabrata.With manipulation of KGDH in Torulopsis glabrata, we screened a mutant strain T. glabrata kgd1:: kan, in which the kgd1 gene encoding the E1 subunit of KGDH was deleted.Disruption of KGDH resulted in: (a) the enhancement of
Dandan, Zhang, Liming, Liu, Guocheng, Du, Jian, Chen   +3 more
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Localization of lipoyl-bearing domains in the .alpha.-ketoglutarate dehydrogenase multienzyme complex

Biochemistry, 1984
The alpha-ketoglutarate dehydrogenase complex from Escherichia coli consists of a core component, dihydrolipoyl transsuccinylase (E2), to which are noncovalently bound 12 polypeptide chains each of alpha-ketoglutarate dehydrogenase and dihydrolipoyl dehydrogenase.
T, Wagenknecht, J, Frank
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Fluorescence polarization study of the .alpha.-ketoglutarate dehydrogenase complex from Escherichia coli

Biochemistry, 1982
The lipoic acids of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli have been modified with two fluorescent probes, N-(1-pyrenyl)-maleimide and 5-[[[(iodoacetyl)amino]ethyl]amino]-naphthylene-1-sulfonic acid. Time-resolved fluorescence polarization of partially labeled complexes (18-77% inhibition of enzyme activity ...
D E, Waskiewicz, G G, Hammes
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pH-Dependent thermodynamic parameters of the glutamate dehydrogenase-α-ketoglutarate-NADPH complex

Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
The enthalpy of formation of the reactive bovine glutamate dehydrogenase-alpha-ketoglutarate-NADPH complex has been measured as a function of pH, at two temperatures and in two buffer systems having different enthalpies of ionization. The results demonstrate the existence of an extensive two-way traffic of protons between the buffer and the complex ...
H F, Fisher, D C, Stickel, A H, Colen
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