Abstract
The E. coli pyruvate dehydrogenase complex, when purified by published procedures, contains phosphotransacetylase and coenzyme A as trace contaminants as well as one or more spectral contaminants which interfere with spectral and radiochemical experiments. They can be removed by further chromatographic purification on columns of calcium phosphate gel-cellulose. The resulting complexes from E. coli K12 or Crookes strain are indistinguishable with respect to visible spectrum, catalytic activity, and flavin content. The activity is the highest so far reported, 40–42 μmoles DPNH per min per mg of protein, and the flavin content is 1.8–2.4 nanomoles per mg of protein.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
