Purification and properties of acetyl coenzyme A synthetase from bovine heart mitochondria.

Acetyl coenzyme A synthetase has been partially purified from many sources including yeast, bacteria, molds, plants, mammalian organs, and pigeon liver (5-11). Substrate amounts of this enzyme, partially purified by the method of Hele from beef heart mitochondria (lo), have been used for the isolation of acetyl adenylate from a reaction mixture containing all reactants except coenzyme A (4). Although the heart preparation provided sufficient adenylate for identification purposes, it was found to contain appreciable activity for the synthesis of butyryl coenzyme A and for the hydrolysis of. chemically synthesized acetyl adenylate (4). For further studies concerning the mechanism of acetate activation, large amounts of an acetyl coenzyme A synthetase, essentially free of butyryl coenzyme A synthetase and acetyl adenylate hydrolase, were needed. This objective has been achieved with the isolation of a nearly homogeneous enzyme and the present paper describes both its purification and some of its characteristics.

• Publication year

  1963

• Venue

  Journal of Biological Chemistry

• Publication date

  1963-05-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(18)81112-7PMID 14018085
• 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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