On the Electrophoretic Behavior of Thermal Polymers of Amino Acids

  • Klaus Dose
  • Horst Rauchfuss


The limited heterogeneity of anumber of thermal polymers of amino acids, also called proteinoids (1), has been established in several reports (2–8). Particularly, if the polymers were subjected to electrophoretic analysis they could be separated into only a small number of definable fractions, mostly three or less. Often electrophoresis even signified true-near-homogeneity. In some instances the single fraction appeared to have a higher degree of homogeneity than even purified organismic proteins. Examples are the acrylamide gel electrophoresis of an unfractionated, but amidated 1:1:1* proteinoid (8) and the gel electrophoresis of a hemoproteinoid (molecular weight about 18.000) which possesses peroxidase-like activity (6–7). However, substantial evidence indicates that electrophoreses is inferior in sensitivity to fractionation on DEAE-Sephadex, DEAE-cellulose, and other cellulose ion exchangers. Fox and Nakashima (8) separated on DEAE-cellulose the amidated 1:1:1 proteinoid into at least three major fractions which all showed identical electrophoretical mobilities. A number of related results which have been obtained in our laboratory are published here.


Aspartic Acid Amino Acid Composition Cellulose Acetate Ammonium Sulfate Amino Acid Mixture 
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.
    Hayakawa, T., Windsor, C. R., and Fox, S. W., Arch. Biochem. Biophys. 118, 265 (1967).CrossRefGoogle Scholar
  2. 2.
    Fox, S. W., and Nakashima, T., Biochem. Biophys. Acta 140, 155 (1967).Google Scholar
  3. 3.
    Vestling, C., in S. W. Fox and K. Harada, J. Am. Chem. Soc. 82, 3745 (1960).Google Scholar
  4. 4.
    Usdin, V. R., Mitz, M. A., and Killos, P. J., Arch. Biochem. Biophys. 122, 258 (1967).CrossRefGoogle Scholar
  5. 5.
    Fox, S. W., Harada, K., Woods, K. R., and Windsor, C. R., Arch. Biochem. Biophys. 102, 439 (1963).PubMedCrossRefGoogle Scholar
  6. 6.
    Dose, K., and Zaki, L., Z. Naturforsch.26b, 144 (1971).Google Scholar
  7. 7.
    Dose, K., and Zaki, L., in “Chemical Evolution and the Origin of Life” (R. Buvet and C. Ponnamperuma, eds.), Molecular Evolution, Vol. 1, North-Holland Publishing Company, Amsterdam, 1971.Google Scholar
  8. 8.
    Fox, S. W., and Nakashima, T., unpublished results.Google Scholar
  9. 9.
    vVeichselbaum, T. E., Amer. J. Clin. Path. (Tech. Sec.) 10, 40 (1946).Google Scholar
  10. 10.
    Gundlach, H. G., Moore, S., and Stein, W. H., J. Biol. Chem. 234, 1754 (1959).PubMedGoogle Scholar
  11. 11.
    Cannan, R. K., Chem. Reviews 30, 395 (1942).CrossRefGoogle Scholar
  12. 12.
    Alberty, R. A., in “The Proteins” (H. Neurath and K. Bailey, eds.) Vol. 1, Part A, p. 484, Academic Press, New York, 1953.Google Scholar
  13. 13.
    Determann, H., “Gelchromatographie, ” Springer-Verlag, BerlinHeidelberg-New York 1967.Google Scholar
  14. 14.
    Maurer, H. R., “Disk-Elektrophorese,” Walter deGruyter & Co., Berlin, 1968.Google Scholar
  15. 15.
    Dose, K., and Risi, S., unpublished results.Google Scholar
  16. 16.
    Rohlfing, D. L., Ph. D. dissertation, Florida State University, 1964.Received 2 August, 1971Google Scholar

Copyright information

© Plenum Press 1972

Authors and Affiliations

  • Klaus Dose
    • 1
  • Horst Rauchfuss
    • 1
  1. 1.Max-Planck-Institut für BiophysikFrankfurt (Main)Germany

Personalised recommendations