Abstract
Monoclonal antibodies specific to the α subunits of the photosynthetic coupling factor 1 (CF1) were used as marker molecules in an electron microscopic analysis of the subunit organization of this enzyme. Immune complexes were obtained by incubation of CF1 with saturating amounts of anti-α-subunit IgG, isolated by gel filtration, and visualized by electron microscopy. The maximum number of antibodies bound to a CF1 molecule was three, the angle defined by a neighboring pair of antibodies characteristically being 120°. These results are interpreted as direct evidence for the presence of three α subunits in the CF1 complex, the relative orientation of them being described by 3-fold rotary symmetry. Our observations thus favor an overall subunit stoichiometry of α3β3γδε.
Keywords: spinach chloroplasts, quaternary protein structure, hybridoma technique
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