Studies on the interaction of Ca2+ ions with some fractions of the neurospecific S-100 protein.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D002118:Calcium / Q000378:metabolism*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011487:Protein Conformation; D009418:S100 Proteins / Q000302:isolation & purification / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D000596:Amino Acids; D009419:Nerve Tissue Proteins; D009418:S100 Proteins; D002118:Calcium