Effect of trypsin on the kinetic properties of reconstituted beef heart cytochromec oxidase

Isolated beef heart cytochromec oxidase was reconstituted in liposomes by the cholate dialysis method with 85% of the binding site for cytochromec oriented to the outside. Trypsin cleaved specifically subunit VIa and half of subunit IV from the reconstituted enzyme. The kinetic properties of the reconstituted enzyme were changed by trypsin treatment if measured by the spectrophotometric assay but not by the polarographic assay. It is concluded that subunit VIa and/or subunit IV participate in the electron transport activity of cytochromec oxidase.