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The ADP,ATP carrier-linked binding protein of beef heart mitochondria was isolated free of ligands, using the detergent 3-lauramido-N,N-dimethylpropylamine oxide. Unlike the preparation of the carboxyatractylate (CAT)-protein complex described earlier, this protein enables direct binding studies to be made with the inhibitor ligands. The protein was characterized with respect to its polypeptide composition, stability against degradation, and immunological properties; the identity of the binding protein with the previously isolated CAT-protein complex was thereby shown. As a step toward reconstitution studies, the isolated binding protein was incorporated into liposomes by a simple rapid mixing process. The complete insertion into the vesicular membrane was demonstrated by chromatography on Sepharose 6B and by immunoprecipitation reactions.
R Krämer, and
H Aquila, and
M Klingenberg
November 1977,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
February 1983,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
October 1982,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
January 1983,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
April 1983,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
December 1987,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
February 1980,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
April 1983,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
November 1986,
Biochemistry,
R Krämer, and
H Aquila, and
M Klingenberg
September 1986,
The Journal of biological chemistry,
