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

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Abstract
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.