title: Presence and stoichiometry of two forms of subunit 6 of the mitochondrial ATPase complex of yeast.
abstract: One of the mitochondrically coded components of the yeast mitochondrial ATPase complex (subunit 6) can be resolved into two components on certain polyacrylamide gels in the presence of sodium dodecyl sulfate. Purification of the ATPase complex from commercially processed yeast as well as immunoprecipitation of the holo-enzyme from cells labeled in vivo with 14C-labeled amino acids demonstrate that both forms of subunit 6 are physically associated with the assembled enzyme and present in two copies each per complex. One-dimensional papain-generated peptide maps of the two components are identical except for the mobility of a single fragment. It is concluded that the two components of subunit 6 are different forms of a single protein and are present on an average of two copies each per complex.
mesh_terms: D000251:Adenosine Triphosphatases / Q000145:classification / Q000302:isolation & purification*; D055598:Chemical Phenomena; D002621:Chemistry; D008928:Mitochondria / Q000201:enzymology*; D010206:Papain; D010446:Peptide Fragments / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
chemical_list: D010446:Peptide Fragments; D010206:Papain; D000251:Adenosine Triphosphatases