Coupling Factor Adenosine-5′-triphosphatase from Rho do spirillum rubrum: A Simple and Rapid Procedure for Its Purification

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Abstract
When photosynthetic membranes from Rhodospirillum rubrum, devoid of loosely bound small molecules and proteins, were passed through a French-pressure cell, the enzyme adenosine-5′-triphosphatase (EC 3.6.1.3.) (ATPase) was released into the soluble fraction. The solubilized ATPase was purified to homogeneity. In many respects it behaved like the enzyme purified by other workers, but it also hydrolyzed Mg-ATP with a small, but significant rate. Furthermore, it was much more stable. Maximal restoration of photophosphorylation in ATPase-depleted membranes was achieved by addition of about 1 mg purified ATPase per mg bacteriochlorophyll. For reconstitution of NAD+- photoreduction, about half of this amount was saturating.

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