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alpha and beta subunits purified from enzyme complex after gel filtration in the presence of 2 M KI followed by chromatography on hydroxyapatite in the presence of 8 M urea
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isolation of EC 1.2.4.1 after elastase treatment of the complex and gel filtration
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Ni2+-Sepharose column chromatography
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purification of pyruvate dehydrogenase complex including pyruvate decarboxylase E1
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purification procedure for the 2-oxoglutarate dehydrogenase and the pyruvate dehydrogenase complexes from mitochondria. After fractionated precipitations with polyethylene glycol, elimination of thiol proteins, and gel-filtration chromatography, the resulting preparations contain both activities. Covalent chromatography on thiol-activated Sepharose CL-4B allows the specific binding of the 2-oxoglutarate dehydrogenase complex activity in the presence of 2-oxoglutarate, the pyruvate dehydrogenase complex activity is retained in the presence of pyruvate
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purification scheme for the pyruvate dehydrogenase complex directly from body wall muscle which yields a fully activated pyruvate dehydrogenase complex with substantial PDHa kinase activity
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pyruvate dehydrogenase can be resolved from complex by incubation with 8 M urea, 4 M guanidinium chloride, 100 mM glycine/NaOH, pH 9.0 followed by gel filtration
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pyruvate dehydrogenase complex composed of EC 1.2. 4.1, EC 2.3.1.12, EC 1.8.1.4
Pigeon
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
pyruvate dehydrogenase complex from ox heart, by PEG fractionation, ultracentrifugation, and gel filtration
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pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
pyruvate dehydrogenase purified from complex by gel filtration
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recombinant multienzyme complex components from Escherichia coli strain BL21(DE3) to homogeneity
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The enzyme complex is resolved into its constituent proteins by means of gel filtration on Sepharose CL-6B in the presence of 2 M-KI, followed by chromatography on hydroxyapatite in the presence of 8 M urea. These harsh conditions are necessary to cause suitable dissociation of the enzyme complex
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
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pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4
Hansenula miso
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pyruvate dehydrogenase complex, composed of EC 1.2.4.1, EC 2.3.1.12, EC 1.8.1.4