1. The purification of an @entity859 triphosphatase present in aqueous extracts of @entity1324 -dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having @entity859 -triphosphatase activity in these extracts. 3. The enzyme is less stable at 0 degrees than at 25 degrees but is stabilized by @entity653 . 4. The activity is dependent on the presence of @entity1025 or certain other bivalent metal cations. 5. The @entity859 -triphosphatase activity of the @entity1025 -activated enzyme is enhanced by @entity3212 . 6. The kinetics of @entity1025 activation indicate that the @entity855 - @entity1025 complex is the important substrate: free @entity855 and @entity1025 are inhibitory. 7. This preparation of mitochondrial @entity859 triphosphatase has many properties in common with the @entity859 triphosphatase coupling factor from mitochondria (Racker, 1961).

Preparation and general properties of a soluble XXXX triphosphatase from mitochondria.

@entity859 :: ('MESH:D000241', 'Chemical') :: ['adenosine'] @entity1025 :: ('CHEBI:18420', 'Chemical') :: ['Mg(2+)'] @entity3212 :: ('MESH:D019297', 'Chemical') :: ['2,4-dinitrophenol'] @entity1324 :: ('MESH:D000096', 'Chemical') :: ['acetone'] @entity653 :: ('MESH:D005990', 'Chemical') :: ['glycerol'] @entity855 :: ('MESH:D000255', 'Chemical') :: ['ATP']
@entity859 :: (MESH:D000241,Chemical) :: ['adenosine']
