Table II LC-MS/MS analysis of proteins released from valinomycin-treated mitochondria

Protein species present in bands B1–3 (supernatant of valinomycin-treated mitochondria) were determined by LC-MS/MS analysis. Those present in the gel pieces in lane A (supernatant of non-treated mitochondria) corresponding to the positions of bands B1–3 were also determined as backgrounds and are shown in the column labeled “Non-treated.” AC, UniProt accession number.

Band no. in lane BIdentified proteinNumber of detected peptidesc (%)d
NameACMolecular massaLocbNon-treatedValinomycin-treated
1Sulfite oxidaseQ0711655IMS18 (38)14 (70)e
Dihydrolipoyl dehydrogenaseQ6P6R255M12 (25)0 (0)
Glutamate dehydrogenase 1P1086062M10 (21)3 (15)
Carbamoyl-phosphate synthaseP07756166M8 (17)3 (15)
2Enoyl-CoA hydrataseP1460432IMS15 (39)7 (26)
Adenylate kinase isoenzyme 2P2941027M11 (29)15 (56)e
Electron transfer flavoprotein subunit βQ68FU328M4 (11)4 (15)
3,2-trans-Enoyl-CoA isomeraseP2396532M3 (6)1 (3)
Hydroxymethylglutaryl-CoA synthaseP2279157M2 (5)0 (0)
3Ribonuclease UK114P5275914Mt, Cy4 (24)4 (15)
Cytochrome cP6289812IMS4 (24)12 (46)e
Hemoglobin subunit β -1P0209112Bl3 (18)3 (12)
Fatty acid-binding protein, liverP0269212Cy3 (18)7 (27)
Hemoglobin subunit αP0194612Bl3 (18)0 (0)
  • a In kDa.

  • b Location of the individual proteins is shown by following abbreviations: Bl, red blood cell; Cy, cytosol; IMS, intermembrane space of mitochondria; M, mitochondrial matrix; Mt, whole mitochondria.

  • c Number of peptides derived from each protein identified by LC-MS/MS analysis.

  • d Relative proportions of the peptide number derived from the protein to the total number of the peptides detected in each protein band are shown.

  • e Peptides (their number and proportion to the total number of peptides) showing predominantly higher proportions in valinomycin-treated mitochondria than in the non-treated mitochondria are underlined.