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Adenosine triphosphatase (ATPase) activities of sonically prepared submitochondrial particles of rat liver and Morris Hepatoma 3924A were compared as a function of changes in temperature. On Arrhenius plots, a discontinuity at 18 degrees was observed for the rat liver mitochondrial ATPase, while the hepatoma mitochondrial ATPase revealed a discontinuity at 20.4 degrees. Values for energy of activation of the rat liver and hepatoma mitochondrial ATPases were comparable below the break (34.5 and 35.5 kcal/mole, respectively) and above the break (11.6 and 9.2 kcal/mole, respectively). Solubilization of the mitochondrial membrances with Triton X-100 resulted in constant and similar values of energy of activation for the ATPases Km values of hepatoma and rat liver mitochondrial ATPases for adenosine triphosphate were similar in both the membrane-bound and solubilized states. The lack of uncoupler-stimulated ATPase activity in hepatoma mitochondria is apparently not due to membranous effects on the affinity of the ATPase for adenosine triphosphate.
R L Melnick, and
R M Hanson, and
H P Morris
December 1989,
Cancer research,
R L Melnick, and
R M Hanson, and
H P Morris
March 1984,
European journal of biochemistry,
R L Melnick, and
R M Hanson, and
H P Morris
April 1984,
FEBS letters,
R L Melnick, and
R M Hanson, and
H P Morris
January 1975,
FEBS letters,
R L Melnick, and
R M Hanson, and
H P Morris
July 1979,
Cancer research,
R L Melnick, and
R M Hanson, and
H P Morris
January 1977,
Neoplasma,
R L Melnick, and
R M Hanson, and
H P Morris
November 1973,
The Journal of biological chemistry,
R L Melnick, and
R M Hanson, and
H P Morris
December 1972,
The Journal of biological chemistry,
R L Melnick, and
R M Hanson, and
H P Morris
January 1977,
Cancer biochemistry biophysics,
R L Melnick, and
R M Hanson, and
H P Morris
October 1970,
Cancer research,
