The Heterogeneity of the S-100 Protein Fraction

  • G. Vincendon
  • J. P. Zanetta
  • G. Gombos
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 32)


It is commonly accepted that the neurospecific protein S-100 is a single molecular species, on the basis of immunological data, and on the basis of its behaviour in several Chromatographic and electrophoretic systems (10) and during analytical ultracentrifugation (15). In fact, the S-100 protein fraction of several animal species migrated as a single band when brain extracts (or the purified protein) were electrophoresed, in the presence of 0.1 mM EDTA, in the Tris-glycine system of Calissano, Moore and Friesen (1). In addition, “S-100 proteins” from the brains of different mammal species, although having somewhat different amino acid compositions (10, 14), appeared to be unusually similar when cross reacting with antiserum to bovine S-100 (10, 13). The precipitin bands neither intersected nor showed “spurs” on a double diffusion test, with the specific antiserum of Levine and Moore (9).


Brain Extract Electrophoretic Profile Dansyl Chloride Immunological Data Peptide Spot 
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Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • G. Vincendon
    • 1
  • J. P. Zanetta
    • 1
  • G. Gombos
    • 1
  1. 1.Centre de Neurochimie du CNRS and Institut de Chimie Biologique, Faculté de Médecine de StrasbourgUniversité Louis-Pasteur67-StrasbourgFrance

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