cytochromes-c1 and n-pentanol

Bovine heart ubiquinol: cytochrome c oxidoreductase in Triton X-100 is split with guanidine into a number of fractions. A new method for measuring antimycin binding is developed using extraction with pentanol of the reversibly bound antimycin. By this method and the normal titration method, antimycin-binding capacity is found in a fraction containing a small subunit with a molecular mass of about 12000. This polypeptide was associated with cytochrome c1 but is probably not the 'hinge protein'. Fractions that contain cytochrome b did not show binding by the pentanol-extraction method.

Topics: Amino Acids; Animals; Antimycin A; Binding Sites; Cattle; Cytochrome b Group; Cytochromes c1; Electron Transport Complex III; In Vitro Techniques; Multienzyme Complexes; Myocardium; NADH, NADPH Oxidoreductases; Pentanols; Quinone Reductases