1887

Abstract

-Hydroxybutyrate dehydrogenase (EC 1.1.1.30) was purified 145-fold from ATCC354 by ammonium sulphate fractionation and DEAE-cellulose chromatography. The pH optima for oxidation and reduction reactions were 8.4 and 6.8 respectively. The purified enzyme was specific for NAD, NADH, acetoacetate and ( − )--hydroxybutyrate. values for --hydroxybutyrate and NAD were 7·4 m and 0.66 mM respectively. The enzyme was inactivated by mercurial thiol inhibitors and by heat, but could be protected by NADH, Ca and partially by Mn. The enzyme did not require metal ions and was insensitive to EDTA, glutathione, dithiothreitol, -mercaptoethanol and cysteine.

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1978-01-01
2024-12-02
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References

  1. Bergmeyer H. U. 1974; 3-Hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides. In Methods of Enzymatic Analysis 1475 Bergmeyer H. U. Edited by New York: Academic Press;
    [Google Scholar]
  2. Bergmeyer H. U., Gawehn K., Klotzsch H. 1967; Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides. Biochemical Journal 102:423–431
    [Google Scholar]
  3. Davis B. J. 1964; Disc electrophoresis. II. Method and application to human serum proteins. Annals of the New York Academy of Sciences 121:404–427
    [Google Scholar]
  4. Delafield F. P., Cooksey K. R., Doudoroff M. 1965; β-Hydroxybutyric acid dehydrogenase and dimer hydrolase of Pseudomonas lemoignei. Journal of Biological Chemistry 240:4023–4028
    [Google Scholar]
  5. Devlin T. M., Bedell B. H. 1960; Effect of acetoacetate on the oxidation of reduced di-phosphopyridine nucleotide by rat liver mitochondria. Journal of Biological Chemistry 235:2134–2139
    [Google Scholar]
  6. Dube S. K., Roholt O., Pressman D. 1963; The chemical nature of the enzyme site of rabbit muscle lactic acid dehydrogenase. Journal of Biological Chemistry 238:613–617
    [Google Scholar]
  7. Lehninger A. L., Sudduth H. C., Wise J.B. 1960; d-β-Hydroxybutyric acid dehydrogenase of mitochondria. Journal of Biological Chemistry 235:2450–2455
    [Google Scholar]
  8. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  9. Okunuki K. 1961; Denaturation and inactivation of enzyme proteins. Advances in Enzymology 23:29–82
    [Google Scholar]
  10. Robert H., Alexander P., Louis H. B. 1973; Model discrimination and nonlinear parameter estimation in the analysis of the mechanism of action of β-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides. Biochimica et biophysica acta 321:1–26
    [Google Scholar]
  11. Senior P. J., Dawes E. A. 1973; The regulation of poly-β-hydroxybutyrate metabolism in Azotobacter beijerinckii. Biochemical Journal 134:225–238
    [Google Scholar]
  12. Shuster C. W., Doudoroff M. 1962; A cold-sensitive D(−)-β-hydroxybutyric acid dehydrogenase from Rhodospirillum rubrum. Journal of Biological Chemistry 237:603–607
    [Google Scholar]
  13. Youmans G. P., Karlson A. G. 1947; Streptomycin sensitivity of tubercle bacilli and the development of resistance to streptomycin in vivo. American Review of Tuberculosis 55:529–535
    [Google Scholar]
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