title: Human milk lactoferrin binds two DNA molecules with different affinities.
abstract: Evidence is presented that lactoferrin (LF), an Fe3+-binding glycoprotein, possesses two DNA-binding sites with different affinities for specific oligonucleotides (ODNs) (Kdl = 8 nM; Kd2 approximately 0.1 mM). The high affinity site became labeled after incubation with affinity probes for DNA-binding sites; like the antibacterial and polyanion-binding sites, this site was shown to be located in the N-terminal domain of LF. Interaction of heparin with the polyanion-binding site inhibits the binding of ODNs to both sites. These data suggest that the DNA-binding sites of LF coincide or overlap with the known polyanion and antimicrobial domains of the protein.
authors.affiliation: Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences.
authors.forename: T G
authors.initials: TG
authors.lastname: Kanyshkova
authors.forename: D V
authors.initials: DV
authors.lastname: Semenov
authors.forename: V N
authors.initials: VN
authors.lastname: Buneva
authors.forename: G A
authors.initials: GA
authors.lastname: Nevinsky
mesh_terms: D000890:Anti-Infective Agents / Q000378:metabolism; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D005260:Female; D006801:Humans; D007781:Lactoferrin / Q000378:metabolism*; D008895:Milk, Human / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D000890:Anti-Infective Agents; D004268:DNA-Binding Proteins; D004247:DNA; D007781:Lactoferrin