Abstract
Digitonin was studied as a means of purifying mitochondrial fractions which were contaminated by lysosomes and other membranous structures. At concentrations which did not cause loss of mitochondrial enzymes, digitonin released into the supernatant significant amounts of marker enzymes for lysosomes, plasma membranes, and other cytoplasmic organelles. Acid glycosidases followed differing patterns of release that may reflect the heterogenous organization of the lysosomal enzyme-membrane complex. While there are limitations to the digitonin method, studies of certain aspects of mitochondrial function may benefit from the digitonin pretreatment step.

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