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Journal of Applied Spectroscopy

, Volume 6, Issue 1, pp 49–50 | Cite as

A spectrofluorimetric study of the interaction of myosin with ATP

  • E. A. Burshtein
Article
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Abstract

Formation of the enzymatically active rnyosin-ATP complex produces a reversible change in the fluorescence of the tryptophan residues, which may be interpreted in terms of a structural rearrangement causing the tryptophan to enter a more hydrophobic environment. Fluorescence is used to follow the kinetics of the formation and decomposition of the enzyme-substrate complex.

Keywords

Analytical Chemistry Molecular Structure Tryptophan Structural Rearrangement Tryptophan Residue 
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.

References

  1. 1.
    J. A. Gally and G. M. Edelman, Biopolymers, 2, Symp. no. 1, 376, 1964.Google Scholar
  2. 2.
    R. F. Steiner, R. E. Lippoldt, H. Edelhoch, and V. Frattali, Biopolymers,2, Symp. no. 1, 33, 1964.Google Scholar
  3. 3.
    E. A. Burshtein, G. M. Zimina, and Yu. A. Vladimirov, ZhPS,4, 142, 1966.Google Scholar
  4. 4.
    Y. Tonomura, K. Sekiya, K. Imamura, and T. Tomonobu, Biochim. Biophys. Acta,69, 305, 1963.Google Scholar
  5. 5.
    E. A. Burshtein and Yu. A. Vladimirov, Biofizika,9, 184, 1964.Google Scholar
  6. 6.
    E. A. Burshtein and T. B. Suslova, in collection: Cell Biophysics [in Russian], Izd. Nauka, Moscow, p. 106, 1965.Google Scholar
  7. 7.
    E. A. Burshtein, in collection: Biophysics of Muscular Contraction [in Russian], Izd. Nauka, Moscow, 1965.Google Scholar
  8. 8.
    L. B. Nanninga, and W. F. H.M. Mommaerts, Proc. Nat. Acad. Sci. USA,46, 1166, 1960.Google Scholar
  9. 9.
    C. C. Bigelow and I. I. Geschwind, C. R. trav. lab Carlsberg, sér chim.,31, 283, 1960.Google Scholar
  10. 10.
    R. E. Davies, Nature,199, 4898, 1068, 1963.Google Scholar

Copyright information

© The Faraday Press, Inc. 1970

Authors and Affiliations

  • E. A. Burshtein

There are no affiliations available

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