[Isolation and properties of CF1 ATPase chloroplasts with changed submolecular structure].

An isolation procedure is worked out and properties are studied of CF1 ATPase from chloroplasts with changed submolecular structure. The enzyme, isolated by chlorophorm treatment, produced Ca-dependent ATPase activity in water solution. As compared with the enzyme isolated by well known Lien and Racker method, the enzyme preparation obtained is slightly activated by heating, is not activated by trypsin and has a lesser ability to recover ATP synthesis in EDTA-treated chloroplasts. Purification on DEAE-Sephadex produced the enzyme preparation free of delta-subunit. Chlorophorm treatment is suggested to change submolecular protein structure, in particular, loosening of the link of delta-subunit with other enzyme subunits. The data obtained suggest that delta-subunit participates in the binding of CF1 ATPase with chloroplast membrane.