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Human milk lactoferrin binds two DNA molecules with different affinities
Author(s) -
Kanyshkova Tat'yana G,
Semenov Dmitry V,
Buneva Valenti,
Nevinsky Georgy A
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00579-7
Subject(s) - lactoferrin , affinities , dna , chemistry , binding affinities , biochemistry , receptor
Evidence is presented that lactoferrin (LF), an Fe 3+ ‐binding glycoprotein, possesses two DNA‐binding sites with different affinities for specific oligonucleotides (ODNs) ( K d1 =8 nM; K d2 ∽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.