Associative properties of butyryl-coenzyme a synthetase from ox liver mitochondria

Robert W. Johnston, Harald Osmundsen, Milton V. Park

    Research output: Contribution to journalArticle

    Abstract

    Butyryl-coenzyme A synthetase (butyrate:CoA ligase (AMP-forming), EC 6.2.1.2) from an acetone-dried powder of ox liver mitochondria was found to have a molecular weight of approx. 40 000. The sedimentation equilibrium analysis suggested the presence in solution of higher molecular weight forms of the enzyme and these could also be obtained by extracting the enzyme from the mitochondrial powder in non-reducing conditions. The enzyme was inhibited by sulphydryl reagents, and was found to have at least one available thiol group/molecule. The relationship between enzymic activity and concentration was non-linear, and suggested that an inactive monomer-active dimer equilibrium was present. The 5-6 fold activation by bovine serum albumin required the presence of free thiol groups in the albumin and involved association of albumin with the enzyme. © 1979.

    Original languageEnglish
    Pages (from-to)70-81
    Number of pages12
    JournalBiochimica et Biophysica Acta (BBA) - Enzymology
    Volume569
    Issue number1
    Publication statusPublished - 11 Jul 1979

    Keywords

    • Activation
    • Albumin
    • Association
    • Butyryl-CoA synthetase
    • Thiol group

    Fingerprint Dive into the research topics of 'Associative properties of butyryl-coenzyme a synthetase from ox liver mitochondria'. Together they form a unique fingerprint.

    Cite this