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Purificaton of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and resolution of its four component polypeptides.

1. The pyruvate dehydrogenase complex was purified from Bacillus stearothermophilus in high yield. The specific activity (about 40nkat/mg of protein) was substantially lower than that of the pyruvate dehydrogenase complex from Escherchia coli (about 570nkat/mg of protein) measured at 30 degrees C un...

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Bibliografische gegevens
Hoofdauteurs: Henderson, C E, Perham, R N
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1980
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1161928/
https://ncbi.nlm.nih.gov/pubmed/7458900
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