Human milk lactoferrin binds ATP and dissociates into monomers

• Published in: Biochemistry and molecular biology international 1999-02, Vol.47 (2), p.177-184
• Main Authors: Semenov, D.V, Kanyshkova, T.g, Buneva, V.N, Nevinsky, G.A
• Format: Article
• Language: English
• Subjects: adenosine triphosphate; Adenosine Triphosphate - metabolism; Affinity Labels; ATP‐binding site localization; Binding Sites; breast milk; Chromatography, Affinity; Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Human milk; Humans; Lactoferrin; Lactoferrin - metabolism; Ligand binding; Milk Proteins - metabolism; Milk, Human - metabolism
• ISSN: 1039-9712; 1521-6543; 1521-6551
• DOI: 10.1080/15216549900201183

The physiological role of lactoferrin (LF) is still unclear, but it has been suggested to be responsible for primary defence against microbial infections. Many different unique functions have been attributed to LF, including DNA and RNA binding, and transport into the nucleus, where LF binds to specific DNA sequences and activates transcription. Here we present evidence that in addition to the above (and below) mentioned functions LF binds ATP with a stoichiometry of 1 mole of nucleotide per mole of the protein and a Kd=0.3 mM. The ATP‐binding site is localized in the C‐terminal domain of LF, in contrast to the antibacterial and polyanion‐binding sites, which are located in the N‐terminal domain. Binding of ATP by LF leads to dissociation of its oligomeric forms and to a change of the protein's interaction with polysaccharides, DNA and proteins.