Specific binding sites for S-100 protein in isolated brain nuclei.
Isolated brain nuclei possess binding sites for S-100 protein. The interaction of S-100 with these sites is specific and time-, temperature-, and Ca+ -dependent. The profile of the (125)I-labelled S-100 binding inhibition is biphasic, displaying a high-affinity component and a low-affinity component. The S-100 binding to brain nuclei is largely irreversible, probably owing to the formation of a tight complex between the protein and its nuclear binding sites. The S-100 binding to brain nuclei is in most aspects similar to that to synaptosomal membranes. Several lines of evidence indicate, however, that the S-100 binding to nuclei is not due to contamination of these structures with plasma membranes. Isolated liver nuclei do not possess the high-affinity component of S-100 binding.
D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000648:ultrastructure*; D002467:Cell Nucleus / Q000378:metabolism*; D005260:Female; D007700:Kinetics; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D009418:S100 Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013574:Synaptosomes / Q000378:metabolism
D009419:Nerve Tissue Proteins; D009418:S100 Proteins