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. 1967 Mar;102(3):801–814. doi: 10.1042/bj1020801

Amino acid sequences of peptides from a tryptic digest of a urea-soluble protein fraction (U.S.3) from oxidized wool

M C Corfield 1, J C Fletcher 1, A Robson 1,*
PMCID: PMC1270331  PMID: 16742497

Abstract

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of the peptides in the digest present in the largest amounts have been determined. 4. The amino acid sequences of 38 of these have been completely elucidated and those of six others partially derived. 5. These findings indicate that the parent protein in wool from which the protein fraction U.S.3 is derived has a minimum molecular weight of 74000. 6. The structures of wool proteins are discussed in the light of the peptide sequences determined, and, in particular, of those sequences in fraction U.S.3 that could not be elucidated.

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Selected References

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  1. AMBLER R. P. THE AMINO ACID SEQUENCE OF PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:349–378. doi: 10.1042/bj0890349. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ATFIELD G. N., MORRIS C. J. Analytical separations by highvoltage paper electrophoresis. Amino acids in protein hydrolysates. Biochem J. 1961 Dec;81:606–614. doi: 10.1042/bj0810606. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CANFIELD R. E. THE AMINO ACID SEQUENCE OF EGG WHITE LYSOZYME. J Biol Chem. 1963 Aug;238:2698–2707. [PubMed] [Google Scholar]
  4. 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]
  5. CORFIELD M. C., ROBSON A. Automatic analysis of amino acids by polarographic estimation of their copper complexes. Biochem J. 1962 Jul;84:146–151. doi: 10.1042/bj0840146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. CORFIELD M. C., SIMPSON E. C. A SENSITIVE SEMI-QUANTITATIVE METHOD FOR AMINO-ACID ANALYSIS. J Chromatogr. 1965 Feb;17:420–425. doi: 10.1016/s0021-9673(00)99892-3. [DOI] [PubMed] [Google Scholar]
  8. Cole M., Fletcher J. C., Robson A. The separation of 1-dimethylaminonaphthalene-5-sulphonamido acids (DNS-amino acids) by thin-layer chromatography. J Chromatogr. 1965 Dec;20(3):616–618. doi: 10.1016/s0021-9673(01)97475-8. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. 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]
  11. Consden R., Gordon A. H., Martin A. J. The identification of lower peptides in complex mixtures. Biochem J. 1947;41(4):590–596. doi: 10.1042/bj0410590. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Fletcher J. C. The reaction of iodobenzene-p-sulphonyl chloride (pipsyl chloride) with certain amino acids and peptides, and with insulin. Biochem J. 1967 Mar;102(3):815–824. doi: 10.1042/bj1020815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  15. MOORE S., STEIN W. H. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J Biol Chem. 1954 Dec;211(2):907–913. [PubMed] [Google Scholar]
  16. Priestley G. C., Speakman P. T. Intra-cellular site of epidermal keratin synthesis. Nature. 1966 Mar 26;209(5030):1336–1337. doi: 10.1038/2091336a0. [DOI] [PubMed] [Google Scholar]
  17. SCHULTZ J., ALLISON H., GRICE M. Specificity of the cleavage of proteins by dilute acid. I. Release of aspartic acid from insulin, ribonuclease, and glucagon. Biochemistry. 1962 Jul;1:694–698. doi: 10.1021/bi00910a024. [DOI] [PubMed] [Google Scholar]
  18. Sanger F. The free amino groups of insulin. Biochem J. 1945;39(5):507–515. doi: 10.1042/bj0390507. [DOI] [PMC free article] [PubMed] [Google Scholar]

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