Human milk lactoferrin binds two DNA molecules with different affinities
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Updated: Aug 18, 2026

Combining Single-molecule Manipulation and Imaging for the Study of Protein-DNA Interactions
Published on: August 27, 2014
T G Kanyshkova1, D V Semenov, V N Buneva
1Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences.
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.
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