1980
DOI: 10.1042/bj1910147
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Purification of 2-oxo acid dehydrogenase multienzyme complexes from ox heart by a new method

Abstract: A new method is described that allows the parallel purification of the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase multienzyme complexes from ox heart without the need for prior isolation of mitochondria. All the assayable activity of the 2-oxo acid dehydrogenase complexes in the disrupted tissue is made soluble by the inclusion of non-ionic detergents such as Triton X-100 or Tween-80 in the buffer used for the initial extraction of the enzyme complexes. The yields of the pyruvate dehydrogenase and… Show more

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Cited by 203 publications
(95 citation statements)
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“…PDC was purified from bovine heart essentially as in [16]. E2 and protein X of PDC, which copurify with each other, were obtained by resolution of the complex using gel filtration on Superose 6 (Pharmacia) in the presence of 1 M NaC1 [9].…”
Section: Methodsmentioning
confidence: 99%
“…PDC was purified from bovine heart essentially as in [16]. E2 and protein X of PDC, which copurify with each other, were obtained by resolution of the complex using gel filtration on Superose 6 (Pharmacia) in the presence of 1 M NaC1 [9].…”
Section: Methodsmentioning
confidence: 99%
“…The pyruvate and 2-oxoglutarate dehydrogenase complexes were prepared from ox heart as in [18], which involves the addition of Triton X-100 to buffers to promote solubilization of the enzymes. The complexes were assayed and their purity confirmed by SDS-polyacrylamide gel electrophoresis in 11.5% Tris-glycine slab gels [18].…”
Section: Methodsmentioning
confidence: 99%
“…The complexes were assayed and their purity confirmed by SDS-polyacrylamide gel electrophoresis in 11.5% Tris-glycine slab gels [18].…”
Section: Methodsmentioning
confidence: 99%
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