ISSN:
1573-6881
Keywords:
F0F1 ATP synthase
;
inhibitor protein
;
protein reconstitution
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract A functional F0F1 ATP synthase that contains the endogenous inhibitor protein (F0F1I) was isolated by the use of two combined techniques [Adolfsen, R., McClung, J.A., and Moudrianakis, E. N. (1975).Biochemistry 14, 1727–1735; Dreyfus, G., Celis, H., and Ramirez, J. (1984).Anal. Biochem. 142, 215–220]. The preparation is composed of 18 subunits as judged by SDS-PAGE. A steady-state kinetic analysis of the latent ATP synthase complex at various concentrations of ATP showed aV max of 1.28Μmol min−1 mg−1, whereas theV max of the complex without the inhibitor was 8.3Μmol min−1 mg−1. In contrast, theK m for Mg-ATP of F0F1 I was 148ΜM, comparable to theK m value of 142ΜM of the F0F1 complex devoid of IF1. The hydrolytic activity of the F0F1I increased severalfold by incubation at 60
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02110338
