Author:
Downes AM,Ferguson KA,Gillespie JM,Harrap BS
Abstract
A study has been made of the incorporation at different levels in the developing fibre of 35S into the two main protein fractions of wool. The proteins have been studied as the S-carboxymethyl derivatives rather than as the oxidized derivatives previously investigated. The results obtained give further support for a mechanism of synthesis which involves two stages. However, the incorporation of some 35S into the low-sulphur fraction of the keratinized fibre only 24 hr after the injection of [35S]cystine is somewhat surprising and possible explanations for this have been considered. A detailed comparison has been made of the proteins extracted from the unkeratinized portions of wool roots by 8M urea with those which can be extracted from the keratinized residue with urea-thioglycollate. As might be expected the latter proteins were very similar to those isolated from wool itself. The group of urea-soluble, high-sulphur proteins was different in containing considerable amounts of protein lower in both molecular weight and sulphur content than the comparable fraction from the fully keratinized wool. The possibility is discussed that some of these urea-soluble, high-sulphur proteins may be precursors of those in the fully keratinized fibre, conversion taking place by a process of sulphur enrichment.
Subject
Developmental Biology,Endocrinology,Genetics,General Materials Science,Molecular Biology,Animal Science and Zoology,Reproductive Medicine,General Medicine,Biotechnology
Cited by
34 articles.
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