Human milk lactoferrin binds two DNA molecules with different affinities

Citation
Tg. Kanyshkova et al., Human milk lactoferrin binds two DNA molecules with different affinities, FEBS LETTER, 451(3), 1999, pp. 235-237
Citations number
23
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
451
Issue
3
Year of publication
1999
Pages
235 - 237
Database
ISI
SICI code
0014-5793(19990528)451:3<235:HMLBTD>2.0.ZU;2-1
Abstract
Evidence is presented that lactoferrin (LF), an Fe3+-binding glycoprotein, possesses two DNA-binding sites with different affinities for specific olig onucleotides (ODNs) (K-d1 = 8 nM; K-d2 similar to 0.1 mM), The high affinit y site became labeled after incubation with affinity probes for DNA-binding sites; like the antibacterial and polyanion-binding sites, this site was s hown to be located in the N-terminal domain of LF. Interaction of heparin w ith 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 wit h the known polyanion and antimicrobial domains of the protein. (C) 1999 Fe deration of European Biochemical Societies.