Internal-Reflection Techniques in Fluorescence Spectroscopy

  • N. J. Harrick
  • G. I. Loeb
Part of the Modern Analytical Chemistry book series (MOAC, volume 1)


Fluorescence techniques have been of great value in situations where the quantity or the nature of samples have required high sensitivity.(1) Investigation of samples of very thin films, of highly absorbing materials where emitted radiation is rapidly attenuated, and of fluid interfaces (such as occur during adsorption from natural environmental and biological fluids) requires the capability of examining surface regions. The combination of fluorescence and internal-reflection techniques can be very useful in such situations. Both single-reflection and multiple-reflection methods have been used.


American Chemical Society Critical Angle Exciting Radiation Angular Spread Unstirred Layer 
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  1. 1.
    S. Udenfriend, Fluorescence Assay in Biology and Medicine (Academic Press, New York, 1962), p. 3.Google Scholar
  2. 2.
    R. W. Wood, Physical Optics, 3rd ed. (Macmillan, New York, 1934).Google Scholar
  3. 3.
    N. J. Harrick, Phys. Rev. Lett. 4, 224 (1960).CrossRefGoogle Scholar
  4. 4.
    N. J. Harrick, Internal Reflection Spectroscopy (Interscience, New York, 1967), pp. 1–15.Google Scholar
  5. 5.
    G. L. Gaines Jr., Insoluble Monolayers at Liquid-Gas Interfaces (Interscience. New York. 1966), p. 110.Google Scholar
  6. 6.
    A. G. Tweet W. D. Bellamy and G. L. Gaines Jr.. J. Chem. Phys. 41. 2068 (1964).CrossRefGoogle Scholar
  7. 7.
    M. N. Kronick and W. A. Little, Bull. Amer. Phys. Soc. 18, 782 (1973).Google Scholar
  8. 8.
    M. N. Kronick and W. A. Little. J. Immunol. Meth. 8. 235 (1975).CrossRefGoogle Scholar
  9. 9.
    L. H. Sharpe, Proc. Chem. Soc. 461, (1961).Google Scholar
  10. 10.
    G. L Loeb, J. Colloid Interface Sci. 26, 236 (1968).CrossRefGoogle Scholar
  11. 11.
    T. Hirschfeld, Can. Spectrosc. 10, 128 (1965).Google Scholar
  12. 12.
    D. J. R. Laurence, Methods Enzymol. 4, 174 (1957).CrossRefGoogle Scholar
  13. 13.
    N. J. Harrick and G. I. Loeb, Anal. Chem. 45, 687 (1973).CrossRefGoogle Scholar
  14. 14.
    K. B. Blodgett, J. Amer. Chem. Soc. 57. 1007 (1935).CrossRefGoogle Scholar
  15. 15.
    H. Sobotka and H. J. Trurnit, “Unimolecular Layers in Protein Analysis.” in Laboratory Manual of Analytical Methods in Protein Chemistry, edited by P. Alexander and R. J. Block (Pergamon Press, Elmsford, N.Y., 1961), Vol. 3, p. 211.Google Scholar
  16. 16.
    I. R. Miller, Progr. Surface Membrane Sci. 4, 299 (1971).Google Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • N. J. Harrick
    • 1
  • G. I. Loeb
    • 2
  1. 1.Harrick Scientific CorporationOssiningUSA
  2. 2.Ocean Sciences DivisionNaval Research LaboratoryUSA

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