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Journal of Solid-Phase Biochemistry

, Volume 3, Issue 1, pp 85–94 | Cite as

Immobilized citrate synthase

  • Amal Mukherjee
  • Paul A. Srere
Article

Abstract

Kinetic properties of pig heart citrate synthase immobilized on Sepharose were determined. Compared to the free enzyme the Km values for both acetyl-CoA and oxalacetate were increased. The kinetic pattern of the Lineweaver-Burk plots of both substrates for the immobilized enzyme was that of lines intersecting on thex axis. This is the same as that obtained for the free enzyme and indicates that there is no change in the kinetic mechanism of the reaction. The pH response and the Arrhenius plot of both the immobilized and free enzyme were the same. The enzymes show a break in their Arrhenius plots. The immobilized enzyme exhibits greater heat stability than does the free enzyme.

Keywords

Immobilize Enzyme Free Enzyme Double Reciprocal Plot Thermal Stability Study Immobilize Enzyme System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Srere, P. A., Mattiasson, B., Mosbach, K. (1973) Proc. Natl. Acad. Sci. U.S.A. 70: 2534.CrossRefGoogle Scholar
  2. 2.
    Simon, E. J., andShemin, D. J. (1953) Am. Chem. Soc. 75: 2520.CrossRefGoogle Scholar
  3. 3.
    Srere, P. A., Brazil, H., andGohen, L. (1963) Acta Chem. Scand. 17: S129.CrossRefGoogle Scholar
  4. 4.
    Kosicki, G. W., andLee, L. P. K. (1966) J. Biol. Chem. 241: 3571.Google Scholar
  5. 5.
    Julliard, J. H., Godinot, C, andGautheron, D. C. (1971) FEBS Lett. 14: 185.CrossRefGoogle Scholar
  6. 6.
    Lilly, M.,Money, C,Hornby, W., andCrook, E. M. (1965) Biochem. J. 95 :45P.Google Scholar
  7. 7.
    Royer, G. P., andGreen, G. M. (1971) Biochem. Biophys. Res. Commun. 44: 426.CrossRefGoogle Scholar
  8. 8.
    Kay, G., andLilly, M. D. (1970) Biochim. Biophys. Acta 198: 276.Google Scholar
  9. 9.
    Matsuoka, Y., andSrere, P. A. (1973) J. Biol. Chem. 248: 8022.Google Scholar
  10. 10.
    Moriyama, T., andSrere, P. A. (1971) J. Biol. Chem. 246: 3217.Google Scholar
  11. 11.
    Weidman, S. W., Drysdale, G. R., andMildvan, A. S. (1971) Fed. Proc. 30: a1294.Google Scholar
  12. 12.
    Johansson, C., andPettersson, G. (1974) Eur. J. Biochem. 42: 383.CrossRefGoogle Scholar
  13. 13.
    Srere, P. A. (1965) Arch. Biochem. Biophys. 110: 200.CrossRefGoogle Scholar
  14. 14.
    Srere, P. A., (1966) J. Biol. Chem. 241: 2147.Google Scholar
  15. 15.
    Eggerer, H. (1965) Biochim. Z. 343: 111.Google Scholar
  16. 16.
    Johansson, C, andPettersson, G. (1974) Eur. J. Biochem. 46: 5.CrossRefGoogle Scholar
  17. 17.
    Weidman, S., Drysdale, G. R., andMildvan, A. S. (1971) Biochemistry 12: 1874.CrossRefGoogle Scholar
  18. 18.
    Mukherjee, A., andSrere, P. A. (1976) J. Biol. Chem. 251: 1476.Google Scholar
  19. 19.
    Cleland, W. W. (1974) Ace. Chem. Res. 8: 145.CrossRefGoogle Scholar
  20. 20.
    Hathaway, J. A., andAtkinson, D. E. (1965) Biochem. Biophys. Res. Commun. 20: 661.CrossRefGoogle Scholar
  21. 21.
    Goldstein, L., Levin, Y., andKatchalski, E. (1964) Biochemistry 3: 1913.CrossRefGoogle Scholar
  22. 22.
    Line, W. E., Kwong, A., andWeetall, H. H. (1971) Biochim. Biophys. Acta 242: 194.Google Scholar
  23. 23.
    Axen, R., andErnback, S. (1971) Eur. J. Biochem. 18: 351.CrossRefGoogle Scholar
  24. 24.
    Brown, E., Racois, A., andGueniffey, H. (1970) Tetrahedron Lett. No. 25: 2139.CrossRefGoogle Scholar
  25. 25.
    Weetall, H. H., andHersh, L. S. (1970) Biochim. Biophys. Acta 206: 54.Google Scholar
  26. 26.
    Stimson, W. H., andSerafini-Fracassini, A. (1971) FEBS Lett. 17: 318.CrossRefGoogle Scholar
  27. 27.
    Cresswell, P., andSanderson, A. R. (1970) Biochem. J. 119: 447.Google Scholar
  28. 28.
    Barker, S. A., Doss, S. H., Gray, C. J., Kennedy, J. F., Stacey, M., andYeo, T. H. (1971) Carbohydr. Res. 20: 1.CrossRefGoogle Scholar
  29. 29.
    Sundaraam, P. V., andHornby, W. E. (1970) FEBS Lett. 10: 325.CrossRefGoogle Scholar
  30. 30.
    Barker, S. A., Somers, P. J., Epton, R., andMcLaren, J. V. (1970) Carbohydr. Res. 14: 287.CrossRefGoogle Scholar
  31. 31.
    Litvak, S., Tarrago-Litvak, L., Carre, D. S., andChapeville, F. (1971) Eur. J. Biochem. 24: 359.CrossRefGoogle Scholar
  32. 32.
    Gabel, D., andHofsten, B. (1970) Eur. J. Biochem. 15: 410.CrossRefGoogle Scholar
  33. 33.
    Matlib, A. M,Finkelstein, M., andSrere, P. A. (1978) Arch. Biochem. Biophys., accepted for publication.Google Scholar

Copyright information

© Humana Press Inc. 1978

Authors and Affiliations

  • Amal Mukherjee
    • 1
  • Paul A. Srere
    • 1
  1. 1.Pre-Clinical Science Unit of Veterans Administration Hospital and Department of BiochemistryUniversity of Texas Health Science CenterDallas

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