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Partial Resolution of the Enzymes Catalyzing Photophosphorylation

IX. STUDIES ON THE SUBUNIT STRUCTURE OF COUPLING FACTOR 1 FROM CHLOROPLASTS

From the ¹ From the Section of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14850

1. Spectrophotometric titration of the tyrosyl residues of coupling factor 1 from spinach chloroplasts with NaOH revealed that approximately one-half of the total tyrosyl groups are located on the surface of the molecules and are readily accessible to the aqueous medium. About onequarter of the tyrosyl residues appear to be located in the intersubunit regions and the remaining quarter of the tyrosyl residues are buried in the hydrophobic region of the subunits.

2. Cold inactivation of coupling factor 1 at mild acid pH in the presence of neutral salts resulted in the dissociation of the protein into subunits. Restoration of over 60% of the Ca²⁺-dependent ATPase and of the coupling factor activity was achieved at 25° provided ATP and 25% glycerol were present.

3. Immunoelectrophoretic analysis of coupling factor 1 under various dissociating conditions indicated the existence of at least two antigenically distinct subunits and the presence of three species of dissociated products with nonidentical electrophoretic mobilities. A specific antibody directed against the native enzyme and not reactive with the subunits was also present in the sera of rabbits after immunization with coupling factor 1.

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