
%0 Journal Article
%A Thompson, EOP 
%A O'donnell, IJ 
%T Studies on Oxidized Wool V. Comparison of Protein Fractions Extracted From Wool by Peptide Mapping of Enzymic Digests
%J Australian Journal of Biological Sciences
%D 1962/09/01
%V 15
%N 3
%P 552-563
%K 
%R https://doi.org/10.1071/BI9620552
%U https://www.publish.csiro.au/paper/BI9620552 
%X Peptide maps, which were prepared by two-dimensional ionophoresis of various enzymic digests of chromatographically resolvable fractions of a-keratose from Merino wool, have failed to reveal any readily detectable differences despite significant differences in amino acid composition. It is postulated that  some contaminant protein which remains bound to the low-sulphur "mother" protein is responsible, in part, for the chromatographic heterogeneity and variation in amino acid composition of separated fractions. Peptide maps of a-keratoses derived from Lincoln and Merino wools are very similar. 
