The125I-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°C, while it is fully reversible after any association time at 4°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 NaC1 or KC1 are more efficient as inhibitors of the S-100 binding to the TX-100 extract than as125I-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.
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Donato, R. Biochemical and physicochemical properties of the solubilized S-100 protein binding activity of synaptosomal particulate fractions. Cell Mol Neurobiol 3, 239–254 (1983). https://doi.org/10.1007/BF00710950
- S-100 protein
- S-100 binding sites
- Ca2+-binding protein