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Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins

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METZ-BOUTIGUE, Marie-Helene, JOLLES, Jacqueline, MAZURIER, Joel, SCHOENTGEN, Francoise, LEGRAND, Dominique, SPIK, Genevieve, MONTREUIL, Jean, JOLLES, Pierre·1984·European Journal of Biochemistry

Abstract

The complete amino acid sequence (703 amino acid residues) of human lactotransferrin has been determined. The location of the disulfide bridges has also been investigated. Computer analysis established internal homology of the two domains (residues 1-338 and residues 339-703). Each domain contains a single iron-binding site and a single glycosylation site (asparagine residues 137 and 490) located in homologous positions. Prediction of the secondary structure of the two homologous moieties of human lactotransferrin has also been performed. The present results allowed a series of comparisons to be made with human serum transferrin and hen ovotransferrin.

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Metadata

Authors
METZ-BOUTIGUE, M.-H., JOLLES, J., MAZURIER, J., SCHOENTGEN, F., LEGRAND, D., SPIK, G., MONTREUIL, J., & JOLLES, P.
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
1984-12
Volume
145
Issue
3
Pages
659-676
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
OpenAlex
W2085338361
Cited by
538
References
0
FWCI
6.58
Type
journal article
Language
en
Open access
bronze

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METZ-BOUTIGUE, M.-H., JOLLES, J., MAZURIER, J., SCHOENTGEN, F., LEGRAND, D., SPIK, G., MONTREUIL, J., & JOLLES, P. (1984). Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1984.tb08607.x

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