title: Human lactotransferrin: molecular, functional and evolutionary comparisons with human serum transferrin and hen ovotransferrin.
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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D003207:Conalbumin; D003553:Cystine / Q000032:analysis; D004220:Disulfides / Q000378:metabolism; D004527:Egg Proteins; D005260:Female; D006801:Humans; D007501:Iron / Q000378:metabolism; D007781:Lactoferrin; D007782:Lactoglobulins; D011134:Polysaccharides / Q000032:analysis; D011487:Protein Conformation; D014168:Transferrin / Q000032:analysis
chemical_list: D000596:Amino Acids; D004220:Disulfides; D004527:Egg Proteins; D007782:Lactoglobulins; D011134:Polysaccharides; D014168:Transferrin; D003207:Conalbumin; D003553:Cystine; D007501:Iron; D007781:Lactoferrin