Soluble Proteins from Fowl Feather Keratin

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 s...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1977-01, Vol.81 (1), p.19-24
Main Authors: MURAYAMA, Kunio, AKAHANE, Kiso, MUROZONO, Soichi
Format: Article
Language:English
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Summary: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 com-ponents 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-cellu-lose was found to be more effective for the isolation of soluble SCM-protetns.
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a131435