Effect of nucleotides on the oligomeric state of human lactoferrin

Autor: S. E. Babina, Valentina N. Buneva, N. A. Tuzikova, G. A. Nevinskii, F. V. Tuzikov
Rok vydání: 2006
Předmět:
Zdroj: Molecular Biology. 40:121-131
ISSN: 1608-3245
0026-8933
DOI: 10.1134/s002689330601016x
Popis: Lactoferrin (LF) is a multifunctional acute-phase protein involved in nonspecific defense against bacteria, viruses, and cancer diseases and is present in human barrier fluids, blood, and milk. Small-angle X-ray scattering (SAXS) and light scattering (LS) demonstrated for the first time that LF occurs in the form of oligomers, with a high monomer unit number in the solution. The degree of LF oligomerization depends on the LF concentration and the storage period of non-frozen neutral LF solutions. The average inertial radius of scattering particles (R g) reaches 100–450 A at LF concentrations comparable with those in human milk, while R g of LF monomers is 26.7 A. LF forms complexes with various nucleotides and hydrolyzes them. The addition of ATP or AMP to LF solutions accelerates LF oligomerization and increases R g to 600–700 A, regardless of the initial degree of LF oligomerization. According to the different models (sphere, plate, and cylinder) of LF aggregates, its complexes with such R g presumably contain several tens to thousands of LF monomers. The possible role of oligomeric complexes in multiple biological functions of LF is discussed.
Databáze: OpenAIRE
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