Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1951 Sep;49(4):554–559. doi: 10.1042/bj0490554

The action of organic acids on some fibrous proteins: the oxidation of wool keratin

S Blackburn 1, A G Lowther 1
PMCID: PMC1197549  PMID: 14886324

Full text

PDF
554

Selected References

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

  1. ALEXANDER P., EARLAND C. Structure of wool fibres; isolation of an alpha and beta-protein in wool. Nature. 1950 Sep 2;166(4218):396–397. doi: 10.1038/166396a0. [DOI] [PubMed] [Google Scholar]
  2. Alexander P., Hudson R. F., Fox M. The reaction of oxidizing agents with wool. 1. The division of cystine into two fractions of widely differing reactivities. Biochem J. 1950 Jan;46(1):27–32. doi: 10.1042/bj0460027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BAMFORD C. H., HANBY W. E., HAPPEY W. E. Solubilities of the alpha II- and beta-forms of synthetic polypeptides: evidence for and alpha II-beta transformation in the amorphous phase. Nature. 1950 Nov 11;166(4228):829–830. doi: 10.1038/166829b0. [DOI] [PubMed] [Google Scholar]
  4. BLACKBURN S. The action of papain on wool keratin. Biochem J. 1950 Oct;47(4):443–451. doi: 10.1042/bj0470443. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bekker J. G., King A. T. Sulphur distribution in the component structures of wool and porcupine quills. Biochem J. 1931;25(4):1077–1080. doi: 10.1042/bj0251077. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Blackburn S. The composition and reactivity of medullated keratins. Biochem J. 1948;43(1):114–117. doi: 10.1042/bj0430114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Consden R., Gordon A. H. A study of the peptides of cystine in partial hydrolysates of wool. Biochem J. 1950 Jan;46(1):8–20. doi: 10.1042/bj0460008. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Consden R., Gordon A. H., Martin A. J. A study of the acidic peptides formed on the partial acid hydrolysis of wool. Biochem J. 1949;44(5):548–560. doi: 10.1042/bj0440548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Consden R., Gordon A. H., Martin A. J. Qualitative analysis of proteins: a partition chromatographic method using paper. Biochem J. 1944;38(3):224–232. doi: 10.1042/bj0380224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Consden R., Gordon A. H., Martin A. J. The identification of amino-acids derived from cystine in chemically modified wool. Biochem J. 1946;40(4):580–582.2. [PMC free article] [PubMed] [Google Scholar]
  11. Dent C. E. A study of the behaviour of some sixty amino-acids and other ninhydrin-reacting substances on phenol-;collidine' filter-paper chromatograms, with notes as to the occurrence of some of them in biological fluids. Biochem J. 1948;43(2):169–180. [PMC free article] [PubMed] [Google Scholar]
  12. HAPPEY F. Polycrystalline structure of wool. Nature. 1950 Sep 2;166(4218):397–398. doi: 10.1038/166397a0. [DOI] [PubMed] [Google Scholar]
  13. SANGER F., TUPPY H. The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates. Biochem J. 1951 Sep;49(4):463–481. doi: 10.1042/bj0490463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sanger F. Fractionation of oxidized insulin. Biochem J. 1949;44(1):126–128. doi: 10.1042/bj0440126. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES