Biochemical and physicochemical properties of the solubilized S-100 protein binding activity of synaptosomal particulate fractions.

The 125I-labeled S-100 specific binding to a Triton X-100 (TX-100) extract of synaptosomal particulate fractions (SYN) was investigated. The results indicate that (a) S-100 binding to the TX-100 extract is partially irreversible after a critical association time at 37 degrees C, while it is fully reversible after any association time at 4 degrees C; (b) trypsin and phospholipase C partially reverse the S-100 binding, while phospholipase D enhances the interaction to some extent, in a dose-dependent way; (c) EDTA and high concentrations of NaCl or KCl are more efficient as inhibitors of the S-100 binding to the TX-100 extract than as 125I-labeled S-100 dissociating agents, in analogy with previous observations with SYN; and (d) two main populations of solubilized S-100 binding sites can be evidenced by gel filtration and sucrose gradient centrifugation when low amounts of the TX-100 extract are processed and/or low S-100 concentrations are used, while two additional molecular species are separated when greater amounts of either factors are tested. These results suggest the possibility that S-100 may be involved in the regulation of some membrane activities.