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. 1971 May;122(4):433–444. doi: 10.1042/bj1220433

Proteins of normal hair and of cysteine-deficient hair from mentally retarded siblings

R J Pollitt 1, P D Stonier 1
PMCID: PMC1176799  PMID: 5166328

Abstract

1. S-Carboxymethylkerateines extracted from normal hair can be fractionated into high-sulphur and low-sulphur proteins similar to those obtained from sheep's wool. Normal human hair gives a major high-sulphur protein of higher molecular weight and S-carboxymethylcysteine content than any isolated from normal sheep's wool. 2. The proteins from cystine-deficient hair can also be divided into high-sulphur and low-sulphur proteins. There is a lower proportion of high-sulphur protein in cystine-deficient hair than in normal hair. 3. The high-sulphur proteins from cystine-deficient hair have an abnormal amino acid composition and in particular are lower in S-carboxymethylcysteine content than the corresponding proteins from normal hair. New components are present and the content of very high-sulphur proteins of high molecular weight is much decreased. The low-sulphur proteins of cystine-deficient hair are probably also deficient in S-carboxymethylcysteine. 4. The proteins of cystine-deficient hair probably resemble those in the normal hair root, except that disulphide-bridge formation has occurred.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brown A. C., Belser R. B., Crounse R. G., Wehr R. F. A congenital hair defect: trichoschisis with alternating birefringence and low sulfur content. J Invest Dermatol. 1970 Jun;54(6):496–509. doi: 10.1111/1523-1747.ep12259317. [DOI] [PubMed] [Google Scholar]
  2. CORFIELD M. C. A new fraction from oxidized wool. Biochem J. 1963 Jan;86:125–129. doi: 10.1042/bj0860125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Corfield M. C., Fletcher J. C., Robson A. Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool. Biochem J. 1967 Mar;102(3):801–814. doi: 10.1042/bj1020801. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Corfield M. C. The fractionation of alpha-keratose. Biochem J. 1962 Sep;84(3):602–610. doi: 10.1042/bj0840602. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Crewther W. G., Harrap B. S. The preparation and properties of a helix-rich fraction obtained by partial proteolysis of low sulfur S-carboxymethylkerateine from wool. J Biol Chem. 1967 Oct 10;242(19):4310–4319. [PubMed] [Google Scholar]
  7. Dale G., Latner A. L. Isoelectric focusing in polyacrylamide gels. Lancet. 1968 Apr 20;1(7547):847–848. doi: 10.1016/s0140-6736(68)90303-6. [DOI] [PubMed] [Google Scholar]
  8. Fraser I. E. Proteins of keratin and their synthesis. II. Incorporation of [35S]cystine into prekeratin and keratin proteins. Aust J Biol Sci. 1969 Feb;22(1):231–238. [PubMed] [Google Scholar]
  9. 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]
  10. Gillespie J. M., Inglis A. S. A comparative study of high-sulphur proteins from alpha-keratins. Comp Biochem Physiol. 1965 Jun;15(2):175–185. doi: 10.1016/0010-406x(65)90345-2. [DOI] [PubMed] [Google Scholar]
  11. Gillespie J. M., Reis P. J. The dietary-regulated biosynthesis of high-sulphur wool proteins. Biochem J. 1966 Mar;98(3):669–677. doi: 10.1042/bj0980669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Leach S. J., Meschers A., Springell P. H. Micro and submicro methods for the estimation of thiol and disulfide groups in insoluble proteins using radioactive mercurials. Anal Biochem. 1966 Apr;15(1):18–30. doi: 10.1016/0003-2697(66)90243-0. [DOI] [PubMed] [Google Scholar]
  13. Pollitt R. J., Jenner F. A., Davies M. Sibs with mental and physical retardation and trichorrhexis nodosa with abnormal amino acid composition of the hair. Arch Dis Child. 1968 Apr;43(228):211–216. doi: 10.1136/adc.43.228.211. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. RACUSEN D., CALVANICO N. PREPARATIVE ELECTROPHORESIS ON POLYACRYLAMIDE GEL. Anal Biochem. 1964 Jan;7:62–66. doi: 10.1016/0003-2697(64)90119-8. [DOI] [PubMed] [Google Scholar]

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