C. Yu, L. Yu
Sep 16, 1980
Citations
0
Influential Citations
31
Citations
Quality indicators
Journal
Biochemical and biophysical research communications
Abstract
Abstract A functionally active arylazido-1-[ 14 C]-β-alanine ubiquinone derivative has been synthesized for the identification of the ubiquinone binding protein in ubiquinol-cytochrome c reductase. After photolysis, the 14C activity was found to be specifically associated to proteins with mobilities relative to cytochrome c of 0.841 and 0.475 in the sodium dodecylsulfate polyacrylamide gel electrophoresis of the Weber and Osborn system. These two proteins have previously been identified as b cytochromes. The 14C activity distribution pattern was observed to be identical in the presence or absence of phospholipids during the photolysis. Antimycin A also produces no change in the 14C activity distribution among the proteins of this enzyme complex.