Abstract
A highly purified and active cytochrome b - c 1 complex has been isolated from the chromatophores of the photosynthetic bacteria Rhodopseudomonas sphaeroides R-26, through steps of Triton X-100 solubilization, salt fractionation and calcium phosphate column chromatography. The isolated enzyme complex catalyzes fully antimycin A sensitive oxidation of ubiquinol by cytochrome c with a turnover number of 1500 per minute at 23° based on cytochrome c 1. It contains 8.3 nmoles of cytochromes b and c 1 per mg protein and shows four polypeptides in the sodium dodecylsulfate polyacrylamide gel electrophoresis.
Full Text 
Sign-in/Register to access full text options
Sign-in/Register to access full text options 
Paper version not known
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
Paper Title
Journal
Date
