Abstract
A soluble fraction of alpha-keratin was obtained on fission of disulphide bonds. The fraction was soluble in the oxidizing solution and would normally be lost when such procedures are used for isolating keratose fractions. This fraction, which constituted 6% by weight of keratin, was rich in cystine, and about 30% of the fraction had a mol.wt. of less than 20 000.
Full text
PDF


Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Buchanan J. H. Use of a programmable pocket calculator in processing amino acid analysis data. J Chromatogr. 1977 Jul 21;137(2):475–480. doi: 10.1016/s0021-9673(00)81373-4. [DOI] [PubMed] [Google Scholar]
- CORFIELD M. C., ROBSON A., SKINNER B. The amino acid compositions of three fractions from oxidized wool. Biochem J. 1958 Feb;68(2):348–352. doi: 10.1042/bj0680348. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Crewther W. G., Fraser R. D., Lennox F. G., Lindley H. The chemistry of keratins. Adv Protein Chem. 1965;20:191–346. doi: 10.1016/s0065-3233(08)60390-3. [DOI] [PubMed] [Google Scholar]
- Gillespie J. M., Broad A. A further study on the dietary-regulated biosynthesis of high-sulphur wool proteins. Biochem J. 1969 Mar;112(1):41–49. doi: 10.1042/bj1120041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lindley H., Haylett T. Occurrence of the Cys-Cys sequence in keratins. J Mol Biol. 1967 Nov 28;30(1):63–67. doi: 10.1016/0022-2836(67)90243-4. [DOI] [PubMed] [Google Scholar]
- Steinert P. M., Rogers G. E. Characterization of the proteins of guinea-pig hair and hair-follicle tissue. Biochem J. 1973 Dec;135(4):759–771. doi: 10.1042/bj1350759. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Zahn H., Biela M. yrosinreiche Proteine im Ameisensäure-Extrakt von reduzierter Wolle. Eur J Biochem. 1968 Sep 24;5(4):567–573. doi: 10.1111/j.1432-1033.1968.tb00407.x. [DOI] [PubMed] [Google Scholar]