, Volume 34, Issue 4, pp 440–441 | Cite as

Quenching of intrinsic fluorescence accompanies the activation of prococoonase

  • Y. Yuthavong


The intrinsic fluorescence of prococoonase fromBombyx mori is largely quenched upon its activation. The rates of fluorescence quenching and enzyme activation are equal, indicating that both reflect the same process.


Enzyme Enzyme Activation Fluorescence Quenching Intrinsic Fluorescence 
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.


  1. 2.
    F. C. Kafatos, A. M. Tartakoff and J. H. Law, J. biol. Chem.242, 1477 (1967).PubMedGoogle Scholar
  2. 3.
    F. C. Kafatos, J. H. Law and A. M. Tartakoff, J. biol. Chem.242, 1477 (1967).PubMedGoogle Scholar
  3. 4.
    E. Berger, F. C. Kafatos, R. L. Felsted and J. H. Law, J. biol. Chem.246, 4131 (1971).PubMedGoogle Scholar
  4. 5.
    R. L. Felsted, K. J. Kramer, J. H. Law, E. Berger and F. C. Kafatos, J. biol. Chem.248, 3012 (1973).PubMedGoogle Scholar
  5. 6.
    K. J. Kramer, R. L. Felsted and J. H. Law, J. biol. Chem.248, 3021 (1973).PubMedGoogle Scholar
  6. 7.
    J. F. Hruska and J. H. Law, Meth. Enzym.19, 221 (1970).Google Scholar
  7. 8.
    F. W. J. Teale, Biochem. J.76, 381 (1960).PubMedGoogle Scholar

Copyright information

© Birkhäuser Verlag 1978

Authors and Affiliations

  • Y. Yuthavong
    • 1
  1. 1.Department of Biochemistry, Faculty of ScienceMahidol UniversityBangkok 4(Thailand)

Personalised recommendations