Soluble proteins from fowl feather keratin. II. Isolation of some proteins from barbs.
Four fractions, GF-1, 2, 3, and 4, which had been separated from S-carboxymethylated (SCM-) proteins of fowl feathers by gel filtration, were each chromatographed on a DEAE-cellulose column in 0.05 M Tris-HCl buffer (pH 8.5) containing 8 M urea. The major fraction, GF-3, was further separated into seven peaks; the first four were shown to be single components by polyacrylamide disc gel electrophoresis. Chromatograms of GF-1 and 2 showed broad peaks which appeared at nearly the same volume as in GF-3. The components from GF-3 had very similar amino acid compositions except that the SCM-cysteine content showed a tendency to increase in the order of elution from the column. SCM-extract prepared from barbs of the wing feathers of a fowl was more heterogeneous than that taken from the body feathers. A combination of gel filtration on Sephadex G-75 and chromatography on DEAE-cellulose was found to be more effective for the isolation of soluble SCM-proteins.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005241:Feathers; D010446:Peptide Fragments / Q000032:analysis; D011506:Proteins / Q000302:isolation & purification*; D012995:Solubility
D000596:Amino Acids; D010446:Peptide Fragments; D011506:Proteins