ISSN:
1573-6830
Keywords:
S-100 protein
;
synaptosomes
;
S-100 binding sites
;
Ca2+-binding protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary 1. The125I-labeled S-100 specific binding to a Triton X-100 (TX-100) extract of synaptosomal particulate fractions (SYN) was investigated. 2. 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. 3. These results suggest the possibility that S-100 may be involved in the regulation of some membrane activities.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00710950
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