Purification and properties of reconstitutively active and inactive adenosinetriphosphatase from XXXX .

@entity1025 @entity526 @entity24427 @entity141 @entity2624 @entity855
The @entity1025 - and @entity141 -stimulated @entity24427 (EC 3.6.1.3; @entity855 phosphohydrolase) (bacterial coupling factor) was purified from two strains of @entity526 by two different procedures: (a) method of Nelson, Kanner, and Gutnick [Proc. Nat. Acad. Sci. USA (1974) 71, 2720-2724] and (b) a modified procedure described in this paper. The @entity24427 purified from @entity2624 (lambda) by the first procedure had 4 subunits (alpha, beta, gamma, and epsilon). It did not bind to a deficient membrane, nor did it reconstitute @entity855 -driven transhydrogenase activity. Our modified procedure (b) yielded 5 subunits (alpha, beta, gamma, delta, and epsilon). This @entity24427 could bind to a deficient membrane and reconstitute @entity855 -driven transhydrogenase. This finding suggests that the delta subunit is required for the reaction with the membrane. The molecular weight of the 4-subunit @entity24427 was significantly lower than that of the 5-subunit @entity24427 , as judged by equilibrium centrifugation. The specific @entity24427 activities of both preparations were about the same. These two procedures were also applied to @entity526 ML308-225.
