1981
DOI: 10.1111/j.1471-4159.1981.tb10814.x
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Studies on the Interaction of Ca2+Ions with Some Fractions of the Neurospecific S‐100 Protein

Abstract: Fractions of neurospecific S-100 protein were purified from bovine brain and their physicochemical properties were studied. Conformational changes caused by the binding of calcium to S-100 protein fractions were detected by means of differential and fluorescence spectroscopy. Fractions demonstrating opposite shifts of their spectra also differ in the distribution in double-phase system. The number of calcium-binding centers and their association. The nature of the differences in the interaction of various S-10… Show more

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Cited by 12 publications
(4 citation statements)
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“…Our data on the effects of A-S-100 in "high" concentrations coincide completely with those obtained earlier at our laboratory (9) and by other authors (3,(10)(11)(12). Ability of A-S-100 to change the excitability of neuronal membrane and to block LTP induction is probably due to the blockage of functional activity of S-100 proteins taking part in regulation of various calcium-depending processes in nervous tissue (13,14).…”
Section: Discussionsupporting
confidence: 91%
See 1 more Smart Citation
“…Our data on the effects of A-S-100 in "high" concentrations coincide completely with those obtained earlier at our laboratory (9) and by other authors (3,(10)(11)(12). Ability of A-S-100 to change the excitability of neuronal membrane and to block LTP induction is probably due to the blockage of functional activity of S-100 proteins taking part in regulation of various calcium-depending processes in nervous tissue (13,14).…”
Section: Discussionsupporting
confidence: 91%
“…Monospecific antiserum to S-100 protein (A-S-100) and non-immune rabbit serum were a generous gift of Dr. S.M.Sviridov. Procedures of S-100 purification and antiserum preparation were described earlier (3). Low concentrations of antibodies were produced using a routine method for homeopathic drugs by «Materia medica» company staff.…”
Section: Experimental and Control Serummentioning
confidence: 99%
“…Antibodies to S-100B were isolated from the serum on columns with S-100B protein immobilized on CNBr-sepharose (17,18). The immunoglobulin solution was dialyzed against 0.15 M NaCl and concentrated using ultrafiltration.…”
Section: Methodsmentioning
confidence: 99%
“…S100A contains and units; S100B contains two units. Procedures of S100 purification and antibody preparation have been described previously (Starostina et al 1981). All dilutions were prepared in glass vials.…”
Section: Elevated Plus-maze Test In the Ratmentioning
confidence: 99%