Figure 4

SDS-PAGE ( panel 1 and 2 ) and Two-dimensional electrophoresis analysis ( panel 3 ) of the cytochrome c ₅₅₃ (a) and cyothcrome oa ₃ oxidase (b) from A. pernix. The acrylamide concentration of the SDS-PAGE gel was 13.5%. The gel was stained for protein with CBB (panel 1) and for heme with o-toluidine in the presence of H₂O₂ (panel 2). The samples were analyzed by BN-PAGE (horizontal) and then SDS-PAGE (vertical, panel 3). A 5-18% acrylamide gradient gel was used for native PAGE, and the gels were stained with CBB. The cytochrome oa₃ oxidase was revealed by its TMPD oxidation activity (b panel 3). The acrylamide concentration of the second dimension SDS-PAGE gel was 15%, and the gels were stained with CBB. Side bars indicate the molecular mass standards. The arrows indicate the corresponding subunits of the cytochrome c₅₅₃ and cytochrome oa₃ oxidase.