The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure.
Open accessAbstract
The amino acid sequences of seven cyanogen bromide fragments of human serum transferrin have been determined, and the primary structure of transferrin established by determining the order of these and three additional fragments (Sutton, M. R., MacGillivray, R. T. A., and Brew, K. (1975) Eur. J. Biochem. 51, 43-48) in the polypeptide chain. The order of the fragments was deduced from peptides that overlap methionyl residues which were obtained by thermolysin digestion of performic acid-oxidized transferrin or by partial peptic hydrolysis of unmodified transferrin, together with other evidence. The polypeptide chain of transferrin contains 679 amino acid residues, which together with the two N-linked oligosaccharide chains gives a calculated molecular weight of 79,570. Transferrin consists of two homologous domains (residues 1-336, 337-679), each associated with a single Fe-binding site, with both sites of glycosylation in the carboxyl-terminal domain at positions 413 and 611. Consideration of the primary structure in relation to previously published results provides information concerning the evolutionary development of transferrins and related proteins, and the locations of metal-binding residues in the transferrin molecule.
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THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID
Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,857
Iron Transport and Storage Proteins
Aisen, P., & Listowsky, I. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002041 · Cited by 1,171
Regeneration of amino acids from thiazolinones formed in the Edman degradation
Méndez, E., & Lai, C. Y. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90677-6 · Cited by 394
Hunkapiller, M. W., & Hood, L. E. (1978) · Biochemistry · doi:10.1021/bi00604a016 · Cited by 383
Brown, E. B. (1977) · Grune & Stratton eBooks · Cited by 282
The Primary Structure of Hen Ovotransferrin
WILLIAMS, J., ELLEMAN, T. C., KINGSTON, I. B., WILKINS, A. G., & KUHN, K. A. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb05880.x · Cited by 204
The Complete Nucleotide Sequence of the Chicken Ovotransferrin mRNA
JELTSCH, J., & CHAMBON, P. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb05879.x · Cited by 183
The complete amino acid sequence of human serum transferrin.
MacGillivray, R. T., Mendez, E., Sinha, S. K., Sutton, M. R., Lineback-Zins, J., & Brew, K. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.8.2504 · Cited by 178
Self-citationThe formation of iron-binding fragments of hen ovotransferrin by limited proteolysis
Williams, J. S. (1974) · Biochemical Journal · doi:10.1042/bj1410745 · Cited by 78
Cited by
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
Antiinflammatory activities of lactoferrin
Conneely, O. M. (2001) · Journal of the American College of Nutrition · doi:10.1080/07315724.2001.10719173 · Cited by 205
Harris, W. R., & Messori, L. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00037-1 · Cited by 145
Bacterial transferrin receptors–structure, function and contribution to virulence
Williams, P., & Griffiths, E. (1992) · Medical Microbiology and Immunology · doi:10.1007/bf00191543 · Cited by 87
Metadata
- Authors
- MacGillivray, R. T., Mendez, E., Shewale, J. G., Sinha, S. K., Lineback-Zins, J., & Brew, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1983-03
- Volume
- 258
- Issue
- 6
- Pages
- 3543-3553
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1575133603
- Cited by
- 275
- References
- 19
- FWCI
- 6.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- MacGillivray, R. T., Mendez, E., Shewale, J. G., Sinha, S. K., Lineback-Zins, J., & Brew, K. (1983). The primary structure of human serum transferrin. The structures of seven cyanogen bromide fragments and the assembly of the complete structure. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)32696-6
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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