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. 2001 Jan;21(2):548–561. doi: 10.1128/MCB.21.2.548-561.2001

FIG. 3.

FIG. 3

Sedimentation properties of mtRNase P. Two equal samples (1 ml) of the UQ fraction from D-treated mitochondria (■) and two equal samples (1 ml) of the UQ fraction from D-plus-MN-treated mitochondria (□) were run in parallel with two samples of bovine liver catalase (1 ml of a 1-mg/ml solution) through 15 to 35% glycerol gradients. After the enzyme activity in the individual fractions of the mtRNase P gradients and the absorbance at 405 nm (Abs405) of the fractions of the catalase gradients were determined, the combined values of the activities of the two mtRNase P samples derived from D-treated mitochondria and of the two samples derived from D-plus-MN-treated mitochondria and the values of absorbance of the two catalase samples were plotted against migration.