The high- and low-sulphur protein fractions are prepared by the reductive fission of the disulphide bonds in the ortho cortex and the paracortex. The amino acid analyses of the kerateine fractions show that the orthocortex is rich in low- sulphur proteins and contains a small fraction of aromatic proteins, while the paracortex has a larger proportion of the high-sulphur protein. The soluble proteins from these two cortices are not extracted completely by a reductive fission, but they are retained to some extent in the insoluble kerateine residues.
Get full access to this article
View all access options for this article.
References
1.
Asquith, R.S. and Parkinson, D.C., TheMorphological Origin and Reactions of Some Keratin Fractions, Textile Res. J.36, 1064-1071 (1966).
2.
Bradbury, J.H. , Chapman, G.V., and King, N.L.R., Chemical Composition of the Histological Components of Wool, in "Symposium on Fibrous Proteins ," Ed., W. G. Crewther, Australia, Butterworths , 1967, pp. 368-372.
3.
Fraser, R.D.B. , Gillespie, J.M., and MacRae, T.P., Tyrosine-Rich Proteins in Keratins, Comp. Biochem. Physiol.44B, 943-947 (1973).
4.
Gillespie, J.M. , Reis, P.J., and Schinckel , P.G., The Isolation andProperties of Some Soluble Proteins from Wool, Aust. J. Biol. Sci.17, 548-560 (1964).
5.
Harrap, B.S. and Gillespie, J.M., A Further Study on the Extraction of Reduced Proteins from Wool, Aust. J. Biol. Sci.16, 542-556 (1963).
6.
Kulkarni, V.G. , Robson, R., and Robson, A., Studies on the Orthocortex and Paracortex of Merino Wool, Appl. Polymer Symp. No. 18, 127-146 (1971).
7.
Piez, K.A. and Morris, L., A Modified Procedure for the Automatic Analysis of Amino Acids, Anal. Biochem.1, 187-201 (1960).