Photon Migration in Muscle and Brain

  • B. Chance
  • D. S. Smith
  • S. Nioka
  • H. Miyake
  • G. Holtom
  • M. Maris


The initial studies of highly scattering biological materials by optical means were made by David Keilin and E.F. Hartree1,2. Using the microspectroscope they observed that the cytochrome absorption bands from various microorganisms, which had been frozen in water or glycerol, were greatly enhanced by micro-recrystallization. Their samples were rapidly frozen in liquid nitrogen, and then rewarmed to a temperature at which a “red halo” was visible in the transmitted light. This produced a better definition of cytochrome absorption bands because of increased light scattering. Furthermore, Keilin showed that the low dispersion microspectroscope gave better visualization of cell and tissue absorption bands than did a higher resolution spectrograph.


Cytochrome Oxidase Exchange Transfusion Pyridine Nucleotide Dual Wavelength Adult Human Brain 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    D. Keilin and E. F. Hartree, Cytochrome and cytochrome oxidase. Proc. Roy. Soc. London B_127: 167–191 (1939).Google Scholar
  2. 2.
    D. Keilin, “The History of Cell Respiration and Cytochrome.” Cambridge University Press, Cambridge, England, 1966.Google Scholar
  3. 3.
    J. Tyndall, “Contributions to Molecular Physics in the Domain of Radiant Heat.” Appleton and Co., NY. Appleton and Co., New York. (1873).Google Scholar
  4. 4.
    G. A. Millikan, Experiments on muscle haemoglobin, Proc. Roy. Soc. London B. 123: 218 (1937).Google Scholar
  5. 5.
    W.L. Butler and K.H. Norris. The spectrophotometry of dense light-scattering material. Arch. Biochem. Biophys. 87:31–40 (1960). See also Smith, K.C. ed. “The Science of Photobiology” Plenum Press, New York, p. 400, 1977.Google Scholar
  6. 6.
    Jobsis, F.F. Non-invasive, infra-red monitoring of cerebral and myocardial oxygen sufficiency and circulatory parameters. Science 198: 1264–1267 (1977).PubMedCrossRefGoogle Scholar
  7. 7.
    P. Kubelka and F. Munk, Ein beitrang zur optik der farbanstriche. Zeits. f. tech. Physik, 12:593 (1931); see also Kubelka, P. New contributions to the optics of light scattering materials. Part I. J. Opt. Soc. Am 38:448 (1948); and Part II. J. Opt. Soc. Am 44: 330 (1954)Google Scholar
  8. 8.
    D. Keilin and E.F. Hartree, Effect of low temperature on the absorption spectra of haemoproteins; with observations on the absorption spectrum of oxygen. Nature London 164: 254 (1949).PubMedCrossRefGoogle Scholar
  9. 9.
    G. A. Millikan, The oximeter, an instrument for measuring continuously the oxygen saturation of arterial blood in man. Rev. Sci. Instrum. 13: 434 (1941).CrossRefGoogle Scholar
  10. 10.
    J. R. Pappenheimer. Vasoconstrictor nerves and oxygen consumption in the isolated perfused hindlimb muscles of the dog. J. Physiol. 99: 184 (1941).Google Scholar
  11. 11.
    H..Lundegardh, Action spectra of the reducing and oxidizing systems in spinach chioroplasts. Biochim. Biophys. Acta 88: 37 (1964).Google Scholar
  12. 12.
    L.M.N. Duysens Thesis, Utrect 1951; see also L.M.N. Duysens, Photosynthesis. In “Progress in Biophysics in Molecular Biology”, Pergamon Press, 1964..Google Scholar
  13. 13.
    E. C. Slater and F.A. Holton, Oxidative phosphorylation coupled with the oxidation of aketoglutarate by heart-muscle sarcosomes. I. Kinetics of the oxidative phosphorylation reaction and adenine nucleotide specificity. Biochem. J. 55: 530 (1953).PubMedGoogle Scholar
  14. 14.
    B. Chance, Rapid and sensitive spectrophotometry Ill. A double beam apparatus. Rev. Sci. lnstrum. 22: 634 (1951).CrossRefGoogle Scholar
  15. 15.
    B. Chance, Enzymes in action in living cells: The steady state of reduced pyridine nucleotide. The Harvey Lecture Series 49: 145 (1955).Google Scholar
  16. 16.
    B. Chance, Enzyme mechanisms in living cells. in: “The Mechanisms of Enzyme Reaction” W. D. McElroy and B. Glass, Eds., The Johns Hopkins Press, Baltimore, pp. 399–453 (1954).Google Scholar
  17. 17.
    B. Chance, Rapid readout from dual wavelength spectrophotometer. Rev. Sci. lnstrum. 43: 62 (1972).CrossRefGoogle Scholar
  18. 18.
    C. M. Connelly and B. Chance, A sensitive spectrophotometric method for reading enzyme reactions in cell suspensions, muscle and nerve. Am. Philos. Soc. 227: 710 (1954).Google Scholar
  19. 19.
    B. Chance and F. Jobsis, Changes in fluorescence in a frog sartorius muscle following a twitch. Nature 184: 195 (1959).CrossRefGoogle Scholar
  20. 20.
    B. Chance and A. Weber, The steady state of cytochrome b during rest and after contraction in frog sartorius. J. Physiol. 169: 263 (1963).PubMedGoogle Scholar
  21. 21.
    L. M. N. Duysens, The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim. Biophys. Acta 19: 1 (1956)PubMedCrossRefGoogle Scholar
  22. 22.
    B. Chance, G. Mauriello, and X.M. Aubert. ADP arrival at muscle following a twitch. In “Muscle as a Tissue” (Rodahl, K. and Horvath, S.M., Eds.) McGraw-Hill Publishers, New York, pp. 128–145 (1961)Google Scholar
  23. 23.
    B. Chance, N. Graham and D. Mayer. A time sharing fluorometry for the read out of intracellular oxidation-reduction states of NADH and flavoprotein. Rev. Sci. lnstru. 42: 951–957 (1971).CrossRefGoogle Scholar
  24. 24.
    H.J. Proctor, A.L. Sylvia and F.F. Jobsis. Failure of brain cytochrome aa3 redox recovery after hypoxic hypotension as determined by in vivo reflectance spectrophotometry. Stroke 13: 89 (1982).PubMedCrossRefGoogle Scholar
  25. 25.
    B. Chance, J.S. Leigh, H. Miyake, D.S Smith, S. Nioka, R. Greenfeld, M. Finander, K. Kaufmann, W.Levy, M. Young, P. Cohen, H. Yoshioka,and R. Boretsky, Comparison of Time Resolved and Unresolved Measurements of Deoxyhemoglobin in Brain. Proc. Nati. Acad. Sci. USA 85: 4971–4975 (1988)CrossRefGoogle Scholar
  26. 26.
    B. Chance, S. Nioka, J. Kent, K. McCully, M. Fountain, R. Greenfeld,and G. Holtom, Time Resolved Spectroscopy of Hemoglobin and Myoglobin Resting and Ischemic Muscle. Anal. Biochem. 174: 698–707 (1988).PubMedCrossRefGoogle Scholar
  27. 27.
    C.L. Bashford, C.H. Barlow, B. Chance and J. Haselgrove. The oxidation-reduction state of cytochrome oxidase in freeze trapped gerbil brains. FEBS Lett. 113: 78–80 (1980).PubMedCrossRefGoogle Scholar
  28. 28.
    P. vanderZee and D.T. Delpy. Computed-point spread functions for light in tissue using a measure volume-scattering function. Intl. Soc. Oxygen Transport to Tisssue (ISOTT) (July 22–25), Sapporo, Japan, p. 82 (1987); see also: P. vanderZee and D.T. Delpy. Simulation of the point spread function for light in tissue by a Monte Carlo technique. Adv. Exp. Med. Biol. 215: 179–192.Google Scholar
  29. 29.
    R. F. Bonner, R. Nossal, S. Havlin and G.H. Weiss, Model for photon migration in turbid biological media. J. Opt. Soc. Am. Sec. A4: 423 (1987)CrossRefGoogle Scholar
  30. 30.
    B. C. Wilson, M. Patterson, S.T. Flock and J.D. Moulton. The optical absorption and scattering of tissues in the visible and near-infrared wavelength range. In “Light in Biology and Medicine” (Douglas, R.H., Moan, J. and dal’Acqua, Eds.) Plenum Publ., New York.Google Scholar
  31. 31.
    W.E. Blumberg, Light propagation in human tissues: The physical origin of the inhomogeneous scattering mechanism. Biophys. J. 51: 288 (1987).Google Scholar
  32. 32.
    O. Hazeki and M. Tamura. The quantitation analysis of hemoglobin oxygenation state of rat brain in situ as monitored by near infra-red spectroscopy. J. Appl. Physioi. 64: 796–802 (1988).Google Scholar
  33. 35.
    Greenfield, R., M.S. Thesis, University of Pennsylvania, Philadelphia, PA 19104Google Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • B. Chance
    • 1
  • D. S. Smith
    • 1
  • S. Nioka
    • 1
  • H. Miyake
    • 1
  • G. Holtom
    • 1
  • M. Maris
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of PennsylvaniaPhiladelphiaUSA

Personalised recommendations