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-100 protein fractions with calcium is discussed.
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Старостина et al. (1981) studied this question.
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