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Using a specific antibody against the PDP catalytic subunit, PDPc, precise localization of this subunit in mitochondria was performed. Sub-fractionation of purified mitochondria by controlled swelling processes led to the isolation of outer membranes, matrix space and inner membrane vesicles which were purified on a sucrose density gradient. In this study, we demonstrated that PDPc was not recovered as a soluble protein in the matrix space but was associated with the inner membrane. Moreover, Triton X-114 phase partitioning performed on inner membranes showed that PDPc behaved both as a hydrophilic and as a hydrophobic protein, thus suggesting two different forms of this enzyme.

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