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Human lactotransferrin: Molecular, functional and evolutionary comparisons with human serum transferrin and hen ovotransferrin

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In this review article, human lactotransferrin is compared to human serum transferrin and hen ovotransferrin. For the first time the possibility of a 6-fold internal homology of the transferrins is raised: a scheme in which 6 domains are defined is reported; two of them with the highest homology seem to be implicated in the 2 iron binding sites of each transferrin. The location of the disulfide bridges of the 3 transferrins and of their prosthetic sugar groups is discussed: some not yet described half-cystine containing lactotransferrin peptides are indicated.

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Authors and Affiliations

  1. Laboratoire de Chimie Biologique et Laboratoire Associé au CNRS, Université des Sciences et Techniques de Lille-I, F-59655, Villeneuve d'Ascq Cedex, France

    J. Mazurier, M. -H. Metz-Boutigue, J. Jollès, G. Spik, J. Montreuil & P. Jollès

  2. Laboratoire des Protéines, Université de Paris V, 45 rue des Saints-Pères, F-75270, Paris Cedex 06, France

    J. Mazurier, M. -H. Metz-Boutigue, J. Jollès, G. Spik, J. Montreuil & P. Jollès

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  1. J. Mazurier
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  2. M. -H. Metz-Boutigue
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  3. J. Jollès
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  4. G. Spik
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  5. J. Montreuil
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  6. P. Jollès
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Acknowledgments. This research was supported by the CNRS (ER No. 102 and LA No. 217) and the INSERM (Unité U-116).

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Mazurier, J., Metz-Boutigue, M.H., Jollès, J. et al. Human lactotransferrin: Molecular, functional and evolutionary comparisons with human serum transferrin and hen ovotransferrin. Experientia 39, 135–141 (1983). https://doi.org/10.1007/BF01958861

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