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. 1968 Jun;108(1):57–67. doi: 10.1042/bj1080057

A comparison of glycopeptides from the ovotransferrin and serum transferrin of the hen

J Williams 1,*
PMCID: PMC1198769  PMID: 5690539

Abstract

1. Glycopeptides were prepared from proteolytic digests of ovotransferrin and serum transferrin of the hen. The carbohydrate compositions and amino acid sequences of the peptides were studied. 2. The bulk of the carbohydrate of ovotransferrin is present as a single oligosaccharide composed of 4 residues of mannose and 8 residues of N-acetylglucosamine. Transferrin has most of its carbohydrate in a single unit composed of 2 residues of mannose, 2 residues of galactose, 3 residues of N-acetylglucosamine and either 1 or 2 residues of sialic acid. 3. The amino acid sequences of the glycopeptides carrying these different oligosaccharides are the same in ovotransferrin and serum transferrin, showing that the carbohydrate groups are attached to the same site on the protein molecule.

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Selected References

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

  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. Brown J. R., Hartley B. S. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. Biochem J. 1966 Oct;101(1):214–228. doi: 10.1042/bj1010214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cunningham L., Ford J. D., Rainey J. M. Heterogeneity of beta-aspartyl-oligosaccharides derived from ovalbumin. Biochim Biophys Acta. 1965 Jul 1;101(2):233–235. [PubMed] [Google Scholar]
  4. 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]
  5. HEILMANN J., BARROLLIER J., WATZKE E. Beitrag zur Aminosäurebestimmung auf Papierchromatogrammen. Hoppe Seylers Z Physiol Chem. 1957;309(4-6):219–220. [PubMed] [Google Scholar]
  6. JAMIESON G. A. STUDIES ON GLYCOPROTEINS. II. ISOLATION OF THE CARBOHYDRATE CHAINS OF HUMAN TRANSFERRIN. J Biol Chem. 1965 Jul;240:2914–2920. [PubMed] [Google Scholar]
  7. KAMINSKI M., DURIEUX J. Etude comparative des sérums de poule, de coq, de poussin, d'embryon et du blanc d'oeuf. Exp Cell Res. 1956 Jun;10(3):590–618. doi: 10.1016/0014-4827(56)90038-6. [DOI] [PubMed] [Google Scholar]
  8. KONIGSBERG W., HILL R. J. The structure of human hemoglobin. III. The sequence of amino acids in the tryptic peptides of the alpha chain. J Biol Chem. 1962 Aug;237:2547–2561. [PubMed] [Google Scholar]
  9. Komatsu S. K., Feeney R. E. Role of tyrosyl groups in metal binding properties of transferrins. Biochemistry. 1967 Apr;6(4):1136–1141. doi: 10.1021/bi00856a024. [DOI] [PubMed] [Google Scholar]
  10. Marks G. S., Marshall R. D., Neuberger A. Carbohydrates in protein. 6. Studies on the carbohydrate-peptide bond in hen's-egg albumin. Biochem J. 1963 May;87(2):274–281. doi: 10.1042/bj0870274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Morgan E. H., Marsaglia G., Giblett E. R., Finch C. A. A method of investigating internal iron exchange utilizing two types of transferrin. J Lab Clin Med. 1967 Mar;69(3):370–381. [PubMed] [Google Scholar]
  12. NUENKE R. H., CUNNINGHAM L. W. Preparation and structural studies of ovalbumin glycopeptides. J Biol Chem. 1961 Sep;236:2452–2460. [PubMed] [Google Scholar]
  13. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  14. PARKER W. C., BEARN A. G. Studies on the transferrins of adult serum, cord serum, and cerebrospinal fluid. The effect of neuraminidase. J Exp Med. 1962 Jan 1;115:83–105. doi: 10.1084/jem.115.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. POULIK M. D. Starch gel electrophoresis in a discontinous system of buffers. Nature. 1957 Dec 28;180(4600):1477–1479. doi: 10.1038/1801477a0. [DOI] [PubMed] [Google Scholar]
  16. RONDLE C. J., MORGAN W. T. The determination of glucosamine and galactosamine. Biochem J. 1955 Dec;61(4):586–589. doi: 10.1042/bj0610586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. SCHROEDER W. A., SHELTON J. R., SHELTON J. B., CORMICK J., JONES R. T. THE AMINO ACID SEQUENCE OF THE GAMMA CHAIN OF HUMAN FETAL HEMOGLOBIN. Biochemistry. 1963 Sep-Oct;2:992–1008. doi: 10.1021/bi00905a016. [DOI] [PubMed] [Google Scholar]
  18. STOFFYN P. J., JEANLOZ R. W. Identification of amino sugars by paper chromatography. Arch Biochem Biophys. 1954 Oct;52(2):373–379. doi: 10.1016/0003-9861(54)90137-x. [DOI] [PubMed] [Google Scholar]
  19. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
  20. WILLIAMS J. Serum proteins and the livetins of hen's-egg yolk. Biochem J. 1962 May;83:346–355. doi: 10.1042/bj0830346. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. WINZLER R. J. Determination of serum glycoproteins. Methods Biochem Anal. 1955;2:279–311. doi: 10.1002/9780470110188.ch10. [DOI] [PubMed] [Google Scholar]
  22. Wenn R. V., Williams J. The isoelectric fractionation of hen's-egg ovotransferrin. Biochem J. 1968 Jun;108(1):69–74. doi: 10.1042/bj1080069. [DOI] [PMC free article] [PubMed] [Google Scholar]

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