The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The Primary Structure of Hen Ovotransferrin
Open accessAbstract
Peptide sequences obtained from hen ovotransferrin are compared with the complete amino acid sequence of the protein deduced from a cDNA sequence (Jeltsch and Chambon, preceding paper). Of the 705 positions of the whole protein 605 can be matched by the peptide sequences. Some possible discrepancies between the two methods are pointed out. The two halves of the chain show marked similarities in their sequences with 37% identical residues. The positions of the 15 disulphide bridges are shown; there are 6 homologous bridges in each half of the molecule and 3 extra bridges which occur only in the C‐terminal half. The terminal residues of the half‐ molecule fragments obtained by limited proteolysis are identified. The two domains are joined by a 9‐residue connecting peptide. Sequence variability has been found at 9 positions. The sequence of hen ovotransferrin IS compared with the partial sequence available for human transferrin. From this some tentative conclusions about the identities of the metal‐binding residues and about the evolution of transferrin are reached.
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Cites
THE PREPARATION OF CRYSTALLINE CONALBUMIN
Warner, R. C., & Weber, I. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50964-9 · Cited by 115
A simple and rapid procedure for preparation of large quantities of pure ovotransferrin
Azari, P., & Baugh, R. F. (1967) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(67)90289-5 · Cited by 71
Cited by
Targeted Drug Delivery via the Transferrin Receptor-Mediated Endocytosis Pathway
Qian, Z. M., Li, H., Sun, H., & Ho, K. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.4.561 · Cited by 1,019
Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins
METZ-BOUTIGUE, M.-H., JOLLES, J., MAZURIER, J., SCHOENTGEN, F., LEGRAND, D., SPIK, G., MONTREUIL, J., & JOLLES, P. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08607.x · Cited by 538
Human transferrin: cDNA characterization and chromosomal localization.
Yang, F., Lum, J. B., McGill, J. R., Moore, C. M., Naylor, S. L., van Bragt, P. H., Baldwin, W. D., & Bowman, B. H. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2752 · Cited by 314
MacGillivray, R. T., Mendez, E., Shewale, J. G., Sinha, S. K., Lineback-Zins, J., & Brew, K. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32696-6 · Cited by 275
Recent advances in the understanding of egg allergens: basic, industrial, and clinical perspectives
Mine, Y., & Yang, M. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8001153 · Cited by 196
Metadata
- Authors
- WILLIAMS, J., ELLEMAN, T. C., KINGSTON, I. B., WILKINS, A. G., & KUHN, K. A.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1982-02
- Volume
- 122
- Issue
- 2
- Pages
- 297-303
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2027981940
- Cited by
- 204
- References
- 2
- FWCI
- 8.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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- WILLIAMS, J., ELLEMAN, T. C., KINGSTON, I. B., WILKINS, A. G., & KUHN, K. A. (1982). The Primary Structure of Hen Ovotransferrin. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1982.tb05880.x
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