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Abstract
Cytochrome c oxidase was isolated from livers and hearts of sheep, dog and rabbit, and the polypeptide composition was analyzed by two different SDS-PAGE separation systems. The gels were blotted on PVDF-membranes and the N-terminal amino acid sequences of the tissue-specific subunits VIa, VIIa and VIII were determined in a protein sequencer. Except for subunit VIIa from rat, subunits VIa and VIIa from all investigated mammals are tissue-specific expressed in liver and heart. In contrast, subunit VIII is clearly different in liver and heart of bovine, dog and rat, but identical in liver and heart of human (liver-type), sheep, rabbit and also in rainbow trout (heart-type). The data suggest a strong species-specific variation of the regulatory properties of cytochrome c oxidase in different tissues.
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Schedule a callMore From: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
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