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 constants were determined by means of equilibrium dialysis and gel filtration. The nature of the differences in the interaction of various S-100 protein fractions with calcium is discussed.