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Sub‐mitochondrial localization of the catalytic subunit of pyruvate dehydrogenase phosphatase
Author(s) -
Simonot Cédric,
Lerme Fabienne,
Louisot Pierre,
Gateau-Roesch Odile
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01461-5
Subject(s) - protein subunit , membrane , inner membrane , inner mitochondrial membrane , biochemistry , chemistry , mitochondrion , intermembrane space , cell fractionation , pyruvate dehydrogenase complex , density gradient , vesicle , mitochondrial matrix , enzyme , biophysics , bacterial outer membrane , biology , cytosol , escherichia coli , physics , quantum mechanics , gene
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.