Abstract
Digestion of the submitochondrial particle (ETPH) with a proteolytic enzyme, Nagarse, selectively and completely removed the headpieces from the membrane without damaging the electron transfer chain. By determining the amount of protein released by the Nagarse treatment, it was calculated that the headpieces represent 16±0.5% of the total protein of the submitochondrial particles.
In respiring ETPH, membrane-bound AMP was found to be an acceptor of inorganic phosphate, and this esterification led to the formation of membrane-bound ADP. About 70% of the membranebound adenine nucleotides were found to be tightly bound to the intrinsic proteins of the membrane. A transphosphorylation reaction was observed between external and membrane-bound ADP.
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Abbreviations
- F1 :
-
coupling factor one
- OSCP:
-
oligomycin-sensitivity conferring protein
- TRU:
-
tripartite repeating unit
- ETPH :
-
phosphorylating electron transfer particle
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Ozawa, T., Asai, J. On the relationship between mitochondrial ATPase and the inner membrane. J Bioenerg Biomembr 4, 507–519 (1973). https://doi.org/10.1007/BF01515942
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DOI: https://doi.org/10.1007/BF01515942