Abstract
Chicken feather powder was solubilized by Schweitzer’s reagent with shaking in the presence of air and the soluble feather keratin was prepared by dialyzing this extract against running water. Cystine residues in the starting feather keratin was converted to cysteic acid residues in the solubilized derivatives by air oxygen. Copper was bound fairly tightly to the solubilized protein and this copper-protein complex was separated into four fractions by CM- and DEAE-cellulose column chromatography. Each fraction had varied amount of bound copper, having a broad distribution of the molecular weight between 10,000 and 60,000 Sephadex column chromatographically. Although the amino acid composition of all separated feather keratin fractions were quite similar, the different electrophoretic patterns were observed among them by DISC electrophoresis.
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