Characterization of detergent-solubilized adenosine triphosphatase of chromaffin granule membranes.

Purified bovine chromaffin granule membranes contain approximately 24 pmol/mg protein (16 copies per granule) of an F1-like adenosine 5'-triphosphatase, and 340 pmol/mg protein (200 copies per granule) of a low-molecular weight protein which reacts covalently with dicyclohexylcarbodiimide. These co-purify on electrofocusing and exclusion chromatography and are apparently components of a proton-translocating adenosine triphosphatase complex, that is involved in maintaining the high concentration of catecholamines in the granules. The membranes contain another adenosine 5'-triphosphatase, of lower molecular weight, which is sensitive to inhibition by vanadate but relatively insensitive to dicyclohexylcarbodiimide. The function of this enzyme is unknown.