Ox liver butyryl-coenzyme a synthetase-a subunit enzyme?

Callum J. Campbell, Milton V. Park

    Research output: Contribution to journalArticle

    Abstract

    1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.

    Original languageEnglish
    Pages (from-to)305-314
    Number of pages10
    JournalInternational Journal of Biochemistry
    Volume16
    Issue number3
    Publication statusPublished - 1984

    Fingerprint

    oxen
    coenzymes
    protein subunits
    ligases
    liver
    enzymes
    guanidines
    isoelectric focusing
    polyacrylamide gel electrophoresis
    polypeptides
    mitochondria
    proteinases
    pigments
    sodium

    Cite this

    Campbell, Callum J. ; Park, Milton V. / Ox liver butyryl-coenzyme a synthetase-a subunit enzyme?. In: International Journal of Biochemistry. 1984 ; Vol. 16, No. 3. pp. 305-314.
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    Campbell, CJ & Park, MV 1984, 'Ox liver butyryl-coenzyme a synthetase-a subunit enzyme?', International Journal of Biochemistry, vol. 16, no. 3, pp. 305-314.

    Ox liver butyryl-coenzyme a synthetase-a subunit enzyme? / Campbell, Callum J.; Park, Milton V.

    In: International Journal of Biochemistry, Vol. 16, No. 3, 1984, p. 305-314.

    Research output: Contribution to journalArticle

    TY - JOUR

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    AU - Campbell, Callum J.

    AU - Park, Milton V.

    PY - 1984

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    N2 - 1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.

    AB - 1. 1. Butyryl-CoA synthetase extracted from untreated or freeze-dried liver mitochondria consisted of two fractions of M, 40,000 and 46,000 as determined by gel permeation chromatography, the higher value Being connrmed Dy sedimentation equilibrium. 2. 2. A red pigment having the characteristics of haem was associated with the enzyme. This appeared to be an artifact of isolation. 3. 3. A number of active bands were obtained on polyacrylamide gel electrophoresis and isoelectric focusing, and on treatment with sodium dodecylsulphate or 6 M guanidine hydrochloride both dissociation and aggregation of the enzyme fractions occurred. 4. 4. As no evidence of protease contamination or proteolytic action could be detected, it is suggested that the active enzymes contain more than one polypeptide chain. © 1984.

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