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Title: Structure and function of the latent F sub 0 -F sub 1 -ATPase complex of Micrococcus lysodeikticus

Thesis/Dissertation ·
OSTI ID:7018896

The latent F{sub 0}F{sub 1}-ATPase from Micrococcus luteus (lysodeikticus) has been purified to homogeneity, and nine distinct subunit bands were observed on SDS-PAGE. Five of nine bands corresponded to the F{sub 1} subunits and the other four bands are likely to be subunits a, a{prime}, b, and c of the F{sub 0} segment of the complex. The subunit designated as a{prime} probably arises from proteolytic cleavage of the 25,5000 Mr subunit a. The F{sub 0}F{sub 1}-ATPase complex has a molecular weight of approximately 1,060,000, as determined by Fast Protein Liquid Chromatography (FPLC). It is assumed that the F{sub 0}F{sub 1}-ATPase peak obtained by FPLC was a dimer and that molecular weight of the F{sub 0}F{sub 1}-ATPase monomer was accordingly 530,000. The stoichiometry of the subunits was determined with {sup 14}C-labeled F{sub 0}F{sub 1}-ATPase prepared from cells grown on medium containing {sup 14}C-amino acids. Antibodies to the native and SDS-denatured F{sub 1} and F{sub 0}F{sub 1}-ATPase as well as to individual SDS-dissociated subunits have been generated for immunochemical analysis. The arrangement of the subunits in F{sub 1} and F{sub 0}F{sub 1}-ATPase have been investigated using bifunctional chemical cross-linking agents.

Research Organization:
New York Univ., NY (USA)
OSTI ID:
7018896
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English