A new preparation of S-100 protein from rat and bovine brains.
The S-100 nervous system protein was purified from bovine and rat brains by a modification of the original procedure. The main modification consisted in substituting a step of calcium-dependent binding of S-100 to a phenyl-Sepharose column for the original step of chromatography on G-200 Sephadex. The proteins were pure as determined by SDS gel electrophoresis. HPLC on a reversed phase and on a size-separation column, and by immunological criteria. The bovine S-100 behaved as previously described, during calcium binding, by displaying a conformational change as evidenced by increase in native fluorescence.
Moore
B W
BW
Washington University School of Medicine, Department of Psychiatry, St. Louis, MO 63110.
Joy
W
W
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002847:Chromatography, Agarose / Q000379:methods*; D002850:Chromatography, Gel / Q000379:methods*; D051381:Rats; D009418:S100 Proteins / Q000302:isolation & purification*; D012685:Sepharose / Q000031:analogs & derivatives
D009418:S100 Proteins; C020927:phenyl-sepharose; D012685:Sepharose