The translocation of energy-rich phosphate in Mycobacterium phlei protoplast ghosts by a soluble protein fraction.

Abstract Oxidative phosphorylation in protoplast ghosts from Mycobacterium phlei was found to be cryptic. The addition of a partially purified soluble protein fraction to the ghost preparations resulted in a transfer of energy-rich phosphate to exogenous ADP. Ghost preparations which were preloaded with [32P]ADP or [14C]ADP resulted in the formation of exogenous [32P]ATP upon the addition of ADP and the soluble protein fraction, whereas [14C]ATP was formed only within the membrane ghost. Sepharose coupled to ADP was used as an external source of ADP to demonstrate the translocation of energy-rich phosphate bond from the inner membrane to the outside upon the addition of the soluble protein fraction.

• Publication year

  1974

• Venue

  Journal of Biological Chemistry

• Publication date

  1974-12-25

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)42069-3PMID 4430684
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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