Human milk lactoferrin binds two DNA molecules with different affinities

FEBS Letters

Semenov, Dmitry V¹  Buneva, Valentina N¹  Kanyshkova, Tat'yana G¹  Nevinsky, Georgy A¹ 

[1] Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of Russian Academy of Sciences, Lavrentieva Ave., 8, Novosibirsk 630090, Russia

关键词: Human milk lactoferrin;    Two DNA-binding sites;    Localization;    LF;    lactoferrin;    ODN;    deoxyribooligonucleotide;    ODN-1;    specific sequence oligonucleotide d(TAGAAGATCAAA);    oxODN;    2′;    3′-dialdehyde derivative of oligonucleotide;   

DOI  :  10.1016/S0014-5793(99)00579-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Evidence is presented that lactoferrin (LF), an Fe³⁺-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.

【 授权许可】

Unknown