Abstract
Vanadate-sensitive ATPase (115 kDa molecular weight) in adrenal chromaffin granules is an intrinsic membrane enzyme with its catalytic site located at the outer surface of the granules. Upon incubation with [γ- 32P]ATP, the purified ATPase formed an alkaline-labile phosphoenzyme intermediate, which was inhibited by vanadate but not by Na + or K +. Ratio of ATPase or phosphatase activity and formation of phosphoenzyme intermediate was constant during purification after the first glycerol density gradient centrifugation. Phosphatidyl-serine specifically activated the enzyme about three-fold by increasing the V max value without changing the K m for ATP. Other phospholipids, including phosphatidyl-glycerol, phosphatidylcholine, phosphatidylinositol, and phosphatidylethanolamine, as well as lysophospholipids and detergents, had no effect. These results indicated that the vanadate-sensitive ATPase belongs to the P-type ATPases, which differ from known cation-translocating P-type ATPases.
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