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IMMUNOCHEMICAL STUDIES OF THE INTERACTION BETWEEN MYELIN BASIC PROTEIN AND S‐100 PROTEIN 1
Author(s) -
Mahadik S. P.,
Graf L.,
Rapport M. M.
Publication year - 1976
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1976.tb12261.x
Subject(s) - polylysine , chemistry , immunoelectrophoresis , polyacrylamide , myelin basic protein , complex formation , major basic protein , bovine serum albumin , biochemistry , biophysics , myelin , biology , antibody , inorganic chemistry , neuroscience , eosinophil , asthma , polymer chemistry , immunology , central nervous system
— The formation of a complex between myelin basic protein and S‐100 protein was detected from the change in migration of S‐100 protein on immunoelectrophoresis. A degree of specificity for the interaction was shown by two observations: (1) two other pure acidic proteins. III‐III‐2 and bovine serum albumin, did not show it and (2) complex formation was dependent on specific ions, either Ca 2+ (10 mM) or Mn 2+ (1 mM). Mg 2+ , Ba 2+ , and Li + had no effect. Non‐specific interactions between S‐100 protein and other basic molecules (histones. polylysine) are not dependent on specific ions such as Ca 2+ and Mn 2+ . The complex was stable at physiological salt concentrations and contained 3 mol of basic protein per mol of S‐100 protein. Complex formation was also detected from the alteration of migration rate of S‐100 protein in polyacrylamide gels. Serological activity (complement‐fixation) of S‐100 protein with anti‐S‐100 serum was reduced in the complex by 30%.