Cross-linking studies on a cytochrome c-cytochrome c oxidase complex. |
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Authors: | M M Briggs R A Capaldi |
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Affiliation: | Institute of Molecular Biology and Department of Biology University of Oregon Eugene, Oregon 97403 USA |
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Abstract: | A cytochrome - cytochrome oxidase complex containing 0.8–1.0 moles of cytochrome per mole of cytochrome oxidase (heme a + a3) was isolated as described by Ferguson-Miller, S., Brautigan, D.L., and Margoliash E., J. Biol. Chem. , 1104 (1976). This complex was reacted with dithiobissuccinimidyl propionate, an 11 Å bridging bifunctional reagent, and the cross-linked products obtained were analyzed by two dimensional gel electrophoresis. Cytochrome was cross-linked to subunit II of cytochrome oxidase. Other cross-linked products were formed involving different subunits of cytochrome oxidase. These included I+V, II+V, III+V, V+VII, IV+VI and IV+VII. Experiments are also described using N,N′-bis(3-succinimidyloxycarbonylpropyl) tartarate. The major product formed with this 18 Å bridging bifunctional reagent was a pair containing II+VI. |
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