title: Orientation of cytochrome c oxidase molecules in the two populations of reconstituted vesicles resolved by column chromatography on DEAE-Sephacryl.
abstract: Vesicles reconstituted with bovine heart cytochrome c oxidase and dioleoylphosphatidylcholine can be resolved into two populations by column chromatography in DEAE-Sephacryl (Madden, T.D. and Cullis, P.R. (1984) J. Biol. Chem. 259, 7655-7658). These two fractions (I and II) were treated with two proteases. These are trypsin, which has been found to cleave subunit IV in the M domain of the cytochrome c oxidase molecule, and chymotrypsin, which has been found to cleave subunit III in the C domain. These studies show that fraction I vesicles contain cytochrome c oxidase orientation with the M domain outside, i.e., in the same topology as in submitochondrial particles, while fraction II vesicles contain enzyme molecules with their C domain outside, and thus in the same orientation as in mitochondria.
authors.forename: Y Z
authors.initials: YZ
authors.lastname: Zhang
authors.forename: R A
authors.initials: RA
authors.lastname: Capaldi
authors.forename: P R
authors.initials: PR
authors.lastname: Cullis
authors.forename: T D
authors.initials: TD
authors.lastname: Madden
mesh_terms: D000818:Animals; D002417:Cattle; D002845:Chromatography; D002918:Chymotrypsin / Q000494:pharmacology; D003576:Electron Transport Complex IV / Q000032:analysis*; D008929:Mitochondria, Heart / Q000201:enzymology; D014357:Trypsin / Q000494:pharmacology
chemical_list: D003576:Electron Transport Complex IV; D002918:Chymotrypsin; D014357:Trypsin