Abstract
Summary The possibility that fast and slow migrating components of S-100 protein fraction, a neurospecific protein, were artifactual, was considered. Several putative causes of artifacts, particularly in relation to conditions of extraction and electrophoresis of brain soluble proteins were examined and ruled out. The two components are neither aggregates nor subunits since they have the same sedimentation coefficients as whole S-100 protein fraction. They are not due to post mortem changes, since there were no differences whether the brain was homogenized immediately or incubated first for 4 h at 37°. Nor are they due to the oxidation of SH-groups, since 2-mercaptoethanol in the extraction buffer or in the electrophoretic system had no effect on the two band pattern. In addition, prerunning of the gels had no effect. Above all, the effect of low (physiological) and high Ca++ ion concentration on the S-100 protein fraction was examined. The two components were not related to the electrophoretic bands induced by Ca++ ions which have been described by certain authors. All the data are in favour of the presence in vivo of fast and slow migrating components of S-100 protein fraction.
Published Version
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