Immobilized Cofactors and Cofactor Fragments in General Ligand Affinity Chromatography and as Active Cofactors

  • K. Mosbach
  • P.-O. Larsson


It is known that many enzymes function only in conjunction with a coenzyme (cofactor) which is generally a compound of low molecular weight. Immobilization of these compounds has been the focus of much effort because of their potential as bioaffinity ligands and in the search for immobilized coenzymes retaining “biological activity”, which are readily retrievable for reuse. Since the first use of adenine nucleotide analogs as general ligands in affinity chromatography (1–3) great progress has been made in the few years that have elapsed (4–8,25). In these studies the adenyl moiety has been chosen for coupling since it is a part of many coenzymes such as ATP, NAD(P)+, FAD and HSCoA.


Affinity Chromatography Alcohol Dehydrogenase Cholic Acid Dependent Enzyme Iodoacetic Acid 
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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  1. 1.
    MOSBACH, K., GUILFORD, H., LARSSON, P.-0., OHLSSON, R. und J. Z25: 20, 1971.Google Scholar
  2. 2.
    LOWE, C.R. und DEAN, P.D.G. Fees Lett. Z4: 313, 1971.CrossRefGoogle Scholar
  3. 3.
    MOSBACH, K., GUILFORD, H., OHLSSON, R. und SCOTT, M. Biochem. J 127: 625, 1972.Google Scholar
  4. 4.
    Mosbach, K. BIOCHEM. Soc. Trans. 2: 1294, 1974.Google Scholar
  5. 5.
    BARRY, S. und O’CARRA, P. Biochem. J. 135: 595, 1973.Google Scholar
  6. 6.
    LEE, C-Y, KAPLAN, N.O. Arch. Biochem. Biophys. 168: 665, 1975.Google Scholar
  7. 7.
    MOSBACH, K. METH. Enzymol. 34: 229, 1974.CrossRefGoogle Scholar
  8. 8.
    Lee, C-Y., LAZARUS, L.H. und KAPLAN, N.O. This volume, p.299.Google Scholar
  9. 9.
    OHLSSON, R., BRODELIUS, P. und MOSBACH, K. Febs Lett. 25: 234, 1972.CrossRefGoogle Scholar
  10. 10.
    GUILFORD, H., LARSSON, P.-0. And MOSBACH, K. Chemica Scripta 2: 165, 1972.Google Scholar
  11. 11.
    BRODELIUS, P., LARSSON, P.-0. and MOSBACH, K. Eur. J. Biochem. 47: 81, 1974.CrossRefGoogle Scholar
  12. 12.
    BRODELIUS, P. und MOSBACH, K. Febs Lett. 35: 223, 1973.CrossRefGoogle Scholar
  13. 13.
    ANDERSSON, L., JORNVALL, H., ?KESON, Â. und MOSBACH, K. BIOCHIM. Biophys. Acta, 364: 1, 1974.CrossRefGoogle Scholar
  14. 14.
    ANDERSSON, L., JORNVALL, H. und MOSBACH, K. Anal. Biochem. 69: 401, 1975.Google Scholar
  15. 15.
    KAPLAN, N.O., EVERSE, J., DIXON, J.E., STOLZENBACH, F.E., LEE, C-Y., Lee, C-L T., TAYLOR, S.S. und MOSBACH, K. PROC. Natl. Acad. Sci. USA, 71: 3450, 1974.CrossRefGoogle Scholar
  16. 16.
    BRODELIUS, P. und Mosbach, K. BIOCHEM. Soc. Trans. 2: 1308, 1974.Google Scholar
  17. 17.
    JERGIL, B., GUILFORD, H. und MOSBACH, K. Biochem. J., 139: 441, 1974.Google Scholar
  18. 18.
    LINDBERG, M., LARSSON, P-0. und MOSBACH, K. EUR. J. Biochem. 40: 187, 1973.CrossRefGoogle Scholar
  19. 19.
    LOWE, C.R. und MOSBACH, K. Eur. J. Biochem. 49: 511, 1974.Google Scholar
  20. 20.
    LINDBERG, M. und MOSBACH, K. Eur. J. Biochem. 53: 481, 1975.Google Scholar
  21. 21.
    LARSSON, P-0. und MOSBACH, K. Febs Lett. 46: 119, 1974.CrossRefGoogle Scholar
  22. 22.
    DAVIES, P. und MOSBACH, K. BIOCHIM. Biophys. Acta, 370: 329, 1974.CrossRefGoogle Scholar
  23. 23.
    GESTRELIUS, S., MLANSSON, M.O., MOSBACH, K. EUR. J. Biochem. 57: 529, 1975.CrossRefGoogle Scholar
  24. 24.
    MOSBACH, K., GESTRELIUS, S. Fees Lett. 42: 200, 1974.CrossRefGoogle Scholar
  25. 25.
    LOWE, C.R. This volume, p. 313.Google Scholar

Copyright information

© Springer Science+Business Media New York 1978

Authors and Affiliations

  • K. Mosbach
    • 1
  • P.-O. Larsson
    • 1
  1. 1.Biochemical Division, Chemical CenterUniversity of LundSweden

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